NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|74184833|dbj|BAE39041|]
View 

unnamed protein product [Mus musculus]

Protein Classification

citrate synthase( domain architecture ID 10149814)

mitochondrial citrate synthase catalyzes the formation of citrate from acetyl-CoA and oxaloacetate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
33-459 0e+00

Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA. In addition to its CS function, ScCit1 plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. Chicken and pig heart CS, two Arabidopsis thaliana (Ath) CSs, CSY4 and -5, and Aspergillus niger (An) CS also belong to this group. Ath CSY4 has a mitochondrial targeting sequence; AthCSY5 has no identifiable targeting sequence. AnCS encoded by the citA gene has both an N-terminal mitochondrial import signal and a C-terminal peroxisiomal target sequence; it is not known if both these signals are functional in vivo. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


:

Pssm-ID: 99858  Cd Length: 427  Bit Score: 961.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  33 LKDVLSNLIPKEQARIKTFKQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGE 112
Cdd:cd06105   1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 113 EPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGMNRA 192
Cdd:cd06105  81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 193 KYWELIYEDCMDLIAKLPCVAAKIYRNLYReGSSIGAIDSRLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 272
Cdd:cd06105 161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 273 HTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRK 352
Cdd:cd06105 240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 353 TDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPNILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGV 432
Cdd:cd06105 320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                       410       420
                ....*....|....*....|....*..
gi 74184833 433 LAQLIWSRALGFPLERPKSMSTDGLMK 459
Cdd:cd06105 400 LSQLIWDRALGLPLERPKSVSTDGLEK 426
 
Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
33-459 0e+00

Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA. In addition to its CS function, ScCit1 plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. Chicken and pig heart CS, two Arabidopsis thaliana (Ath) CSs, CSY4 and -5, and Aspergillus niger (An) CS also belong to this group. Ath CSY4 has a mitochondrial targeting sequence; AthCSY5 has no identifiable targeting sequence. AnCS encoded by the citA gene has both an N-terminal mitochondrial import signal and a C-terminal peroxisiomal target sequence; it is not known if both these signals are functional in vivo. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


Pssm-ID: 99858  Cd Length: 427  Bit Score: 961.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  33 LKDVLSNLIPKEQARIKTFKQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGE 112
Cdd:cd06105   1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 113 EPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGMNRA 192
Cdd:cd06105  81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 193 KYWELIYEDCMDLIAKLPCVAAKIYRNLYReGSSIGAIDSRLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 272
Cdd:cd06105 161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 273 HTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRK 352
Cdd:cd06105 240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 353 TDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPNILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGV 432
Cdd:cd06105 320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                       410       420
                ....*....|....*....|....*..
gi 74184833 433 LAQLIWSRALGFPLERPKSMSTDGLMK 459
Cdd:cd06105 400 LSQLIWDRALGLPLERPKSVSTDGLEK 426
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
30-457 0e+00

citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal forms of citrate synthase. Citrate synthase is the entry point to the TCA cycle from acetyl-CoA. Peroxisomal forms, such as SP:P08679 from yeast (recognized by the C-terminal targeting motif SKL) act in the glyoxylate cycle. Eukaryotic homologs excluded by the high trusted cutoff of this model include a Tetrahymena thermophila citrate synthase that doubles as a filament protein, a putative citrate synthase from Plasmodium falciparum (no TCA cycle), and a methylcitrate synthase from Aspergillus nidulans.


Pssm-ID: 130853  Cd Length: 427  Bit Score: 781.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833    30 STNLKDVLSNLIPKEQARIKTFKQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAK 109
Cdd:TIGR01793   1 DLDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   110 GGEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGM 189
Cdd:TIGR01793  81 GGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   190 NRAKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIgAIDSRLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGN 269
Cdd:TIGR01793 161 HKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSI-SIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   270 VSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAV 349
Cdd:TIGR01793 240 VSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   350 LRKTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPNILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA 429
Cdd:TIGR01793 320 LRKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRA 399
                         410       420
                  ....*....|....*....|....*...
gi 74184833   430 LGVLAQLIWSRALGFPLERPKSMSTDGL 457
Cdd:TIGR01793 400 LGILSQLIWDRALGLPLERPKSVSTEWL 427
PRK09569 PRK09569
citrate (Si)-synthase;
33-464 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 609.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   33 LKDVLSNLIPKEQARIKTFKQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGE 112
Cdd:PRK09569   3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  113 EPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEG-MNR 191
Cdd:PRK09569  83 YPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGkFNK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  192 AKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIgAIDSRLDWSHNFTNMLGYtDPQFTELMRLYLTIHSDHEGGNVS 271
Cdd:PRK09569 163 MDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQI-PSDPELDYGANFAHMIGQ-PKPYKDVARMYFILHSDHESGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  272 AHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEV-GKDVSDEKLRDYIWNTLNSGRVVPGYGHAVL 350
Cdd:PRK09569 241 AHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKLgGEEPTKEQVEQALWDTLNAGQVIPGYGHAVL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  351 RKTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPNILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRAL 430
Cdd:PRK09569 321 RKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRAL 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 74184833  431 GVLAQLIWSRALGFPLERPKSMSTDGLMKFVDSK 464
Cdd:PRK09569 401 GVMANITWDRGLGYAIERPKSVTTEMLEKWAAEG 434
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
71-450 7.29e-130

Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.


Pssm-ID: 459747 [Multi-domain]  Cd Length: 357  Bit Score: 379.93  E-value: 7.29e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833    71 GMRGMKGLVYETSVLDPDEG-IRFRGYSIPE-CQKMLPkakggeeplpEGLFWLLVTGQMPTEEQVSWLSREWAKRAALP 148
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEElAERSSF----------EEVAYLLLTGELPTKEELEEFSAELAAHRELP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   149 SHVVTMLDNFPTNLHPMSQLSAAITALNSESNFArayaeGMNRAKYWELIYEDcmDLIAKLPCVAAKIYRnlYREGSSIG 228
Cdd:pfam00285  71 EDVLELLRALPRDAHPMAVLRAAVSALAAFDPEA-----ISDKADYWENALRD--DLIAKLPTIAAYIYR--HRRGLPPI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   229 AIDSRLDWSHNFTNML-GYT-DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 306
Cdd:pfam00285 142 YPDPDLSYAENFLYMLfGYEpDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   307 EVLVWLTQLQKEvgkdvsdEKLRDYIWNTLNSG-RVVPGYGHAVLRKTDPRYSCQREFALKHLPK---DPMFKLVAQLYK 382
Cdd:pfam00285 221 AVLEMLEEIGSP-------DEVEEYIRKVLNKGkERIMGFGHRVYKNYDPRAKILKEFAEELAEEggdDPLLELAEELEE 293
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74184833   383 IVPNILLEQGkaKNPWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQLIWSRALGfPLERPK 450
Cdd:pfam00285 294 VAPEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
62-451 2.04e-103

Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440141 [Multi-domain]  Cd Length: 387  Bit Score: 313.57  E-value: 2.04e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  62 QITVDMMYGGMRGMKG-LVYETSV--LDPDEGI-RFRGYSIPECQkmlpkakggEEPLPEGLFWLLVTGQMPTEEQVSWL 137
Cdd:COG0372   4 EIDIRAKFTVDPGLEGvVAGETAIsyIDGEKGIlRYRGYPIEDLA---------EKSSFEEVAYLLLYGELPTKEELAEF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 138 SREWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALnseSNFaraYAEGMNRAKywELIYEDCMDLIAKLPCVAAKIY 217
Cdd:COG0372  75 KAELARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSAL---GAF---DPDADDIDP--EARLEKAIRLIAKLPTIAAYAY 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 218 RnlYREGSSIGAIDSRLDWSHNFTNMLGYT--DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNG 295
Cdd:COG0372 147 R--YRRGLPPVYPDPDLSYAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGA 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 296 LAGPLHGLANQEVLVWLtqlqKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHLPKDP 372
Cdd:COG0372 224 LKGPLHGGANEAVLEML----EEIG---SPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDP 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 373 MFKLVAQLYKIVPNilLEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRAlGFPLERPKS 451
Cdd:COG0372 297 LLEIAEELEEVALE--DEYFIEKKLYPNVDFYSGIVYHALGIpTDM--FTPIFAISRVAGWIAHWLEQRA-DNRIIRPRQ 371
 
Name Accession Description Interval E-value
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
33-459 0e+00

Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA. In addition to its CS function, ScCit1 plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. Chicken and pig heart CS, two Arabidopsis thaliana (Ath) CSs, CSY4 and -5, and Aspergillus niger (An) CS also belong to this group. Ath CSY4 has a mitochondrial targeting sequence; AthCSY5 has no identifiable targeting sequence. AnCS encoded by the citA gene has both an N-terminal mitochondrial import signal and a C-terminal peroxisiomal target sequence; it is not known if both these signals are functional in vivo. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


Pssm-ID: 99858  Cd Length: 427  Bit Score: 961.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  33 LKDVLSNLIPKEQARIKTFKQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGE 112
Cdd:cd06105   1 LKDRLAELIPKEQARIKKFRKEHGKTVVGEVTVDMVYGGMRGIKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAPGGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 113 EPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGMNRA 192
Cdd:cd06105  81 EPLPEGLFWLLLTGEVPTKEQVSALSKEWAARAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESKFAKAYAEGIHKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 193 KYWELIYEDCMDLIAKLPCVAAKIYRNLYReGSSIGAIDSRLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 272
Cdd:cd06105 161 KYWEYVYEDSMDLIAKLPCVAAKIYRNLYR-GGKIIAIDSNLDWSANFANMLGYTDPQFTELMRLYLTIHSDHEGGNVSA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 273 HTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRK 352
Cdd:cd06105 240 HTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTKLQKEVGKDVSDEQLREYVWKTLNSGRVVPGYGHAVLRK 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 353 TDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPNILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGV 432
Cdd:cd06105 320 TDPRYTCQREFALKHLPNDPLFKLVSQLYKIVPPVLTEQGKAKNPWPNVDAHSGVLLQYYGLTEMNYYTVLFGVSRALGV 399
                       410       420
                ....*....|....*....|....*..
gi 74184833 433 LAQLIWSRALGFPLERPKSMSTDGLMK 459
Cdd:cd06105 400 LSQLIWDRALGLPLERPKSVSTDGLEK 426
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
33-457 0e+00

Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). This group includes three S. cerevisiae CS proteins, ScCit1,-2,-3. ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA; in addition to having activity with AcCoA, it plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. ScCit3 is a mitochondrial CS and functions in the metabolism of PrCoA; it is a dual specificity CS and 2MCS, having similar catalytic efficiency with both AcCoA and PrCoA. The pattern of expression of the ScCIT3 gene follows that of the ScCIT1 gene and its expression is increased in the presence of a ScCIT1 deletion. Included in this group is the Tetrahymena 14 nm filament protein which functions as a CS in mitochondria and as a cytoskeletal component in cytoplasm and Geobacter sulfurreducens (GSu) CS. GSuCS is dimeric and eukaryotic-like; it lacks 2MCS activity and is inhibited by ATP. In contrast to eukaryotic and other prokaryotic CSs, GSuCIT is not stimulated by K+ ions. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


Pssm-ID: 99857  Cd Length: 426  Bit Score: 810.37  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  33 LKDVLSNLIPKEQARIKTFKQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGE 112
Cdd:cd06103   1 LKDKLAELIPKKQARIKELRKKYGNTKLGQITVDQVIGGMRGMKGLVYETSVLDPDEGIRFRGKTIPECQELLPKADGGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 113 EPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEG-MNR 191
Cdd:cd06103  81 EPLPEGLFWLLLTGEVPTEEQVDELSKEWAKRAEVPSHVVKMIDNLPRNLHPMTQLSAAILALQSESKFAKAYAEGkINK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 192 AKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIGAIDSRLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVS 271
Cdd:cd06103 161 TTYWEYVYEDAMDLIAKLPVVAAKIYRRKYRKGGEIGAIDSKLDWSANFAHMLGYEDEEFTDLMRLYLTLHSDHEGGNVS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 272 AHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLR 351
Cdd:cd06103 241 AHTSHLVGSALSDPYLSFSAALNGLAGPLHGLANQEVLKWLLKMQKELGKDVSDEELEKYIWDTLNSGRVVPGYGHAVLR 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 352 KTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPNILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALG 431
Cdd:cd06103 321 KTDPRFTCQREFALKHLPDDPLFKLVAQCYKIIPGVLKEHGKVKNPYPNVDAHSGVLLQHYGMTEPQYYTVLFGVSRALG 400
                       410       420
                ....*....|....*....|....*.
gi 74184833 432 VLAQLIWSRALGFPLERPKSMSTDGL 457
Cdd:cd06103 401 VLAQLVWSRALGLPIERPKSMSTEGL 426
cit_synth_euk TIGR01793
citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal ...
30-457 0e+00

citrate (Si)-synthase, eukaryotic; This model includes both mitochondrial and peroxisomal forms of citrate synthase. Citrate synthase is the entry point to the TCA cycle from acetyl-CoA. Peroxisomal forms, such as SP:P08679 from yeast (recognized by the C-terminal targeting motif SKL) act in the glyoxylate cycle. Eukaryotic homologs excluded by the high trusted cutoff of this model include a Tetrahymena thermophila citrate synthase that doubles as a filament protein, a putative citrate synthase from Plasmodium falciparum (no TCA cycle), and a methylcitrate synthase from Aspergillus nidulans.


Pssm-ID: 130853  Cd Length: 427  Bit Score: 781.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833    30 STNLKDVLSNLIPKEQARIKTFKQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAK 109
Cdd:TIGR01793   1 DLDLKEQLKEKIPEQQEKVKKLRAEHGKVVLGNITVDMVYGGMRGMKGLVWETSVLDPEEGIRFRGLSIPECQKLLPKAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   110 GGEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGM 189
Cdd:TIGR01793  81 GGEEPLPEGLLWLLLTGKVPSEEQVDALSAEWRARADLPEHVYKTIDALPVTLHPMAQFATAVMALQVESEFAKAYAKGI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   190 NRAKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIgAIDSRLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGN 269
Cdd:TIGR01793 161 HKTKYWEYTYEDSMDLIAKLPTVAAYIYRNMYKDGQSI-SIDDSKDYSANFAHMLGYDSPSFQELMRLYLTIHSDHEGGN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   270 VSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAV 349
Cdd:TIGR01793 240 VSAHTGHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLLWLKSVVSECGENVTKEQLKDYIWKTLNSGKVVPGYGHAV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   350 LRKTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPNILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA 429
Cdd:TIGR01793 320 LRKTDPRYICQREFALKHLPDDPLFKLVSNLYKIVPGILTELGKVKNPWPNVDAHSGVLLQYYGLTEARYYTVLFGVSRA 399
                         410       420
                  ....*....|....*....|....*...
gi 74184833   430 LGVLAQLIWSRALGFPLERPKSMSTDGL 457
Cdd:TIGR01793 400 LGILSQLIWDRALGLPLERPKSVSTEWL 427
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
33-457 0e+00

Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase (2MCS) catalyzes the condensation of propionyl-coenzyme A (PrCoA) and oxaloacetate (OAA) to form 2-methylcitrate and CoA. Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with OAA to form citrate and CoA, the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit3 is mitochondrial and functions in the metabolism of PrCoA; it is a dual specificity CS and 2MCS, having similar catalytic efficiency with both AcCoA and PrCoA. The pattern of expression of the ScCIT3 gene follows that of the major mitochondrial CS gene (CIT1, not included in this group) and its expression is increased in the presence of a CIT1 deletion. This group also contains Aspergillus nidulans 2MCS; a deletion of the gene encoding this protein results in a strain unable to grow on propionate. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


Pssm-ID: 99859  Cd Length: 428  Bit Score: 634.54  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  33 LKDVLSNLIPKEQARIKTFKQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGE 112
Cdd:cd06106   1 LKEALKEVIPAKREQLKKLKAEYGETVVGDVKVSNVLGGMRGLKSMLWEGSVLDAEEGIRFHGKTIPECQKELPKAPIGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 113 EPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGMNRA 192
Cdd:cd06106  81 EMLPESMLWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKTLHPMTQLSIGVAALNHDSKFAAAYEKGIKKT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 193 KYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIGAIDSRLDWSHNFTNMLGYTDPQ-FTELMRLYLTIHSDHEGGNVS 271
Cdd:cd06106 161 EYWEPTLEDSLNLIARLPALAARIYRNVYGEGHGLGKIDPEVDWSYNFTSMLGYGDNLdFVDLLRLYIALHGDHEGGNVS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 272 AHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLR 351
Cdd:cd06106 241 AHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRWILEMQKNIGSKATDQDIRDYLWKTLKSGRVVPGYGHAVLR 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 352 KTDPRYSCQREFALKH--LPKDPMFKLVAQLYKIVPNILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA 429
Cdd:cd06106 321 KPDPRFTALMEFAQTRpeLENDPVVQLVQKLSEIAPGVLTEHGKTKNPFPNVDAASGVLFYHYGIREFLYYTVIFGVSRA 400
                       410       420
                ....*....|....*....|....*...
gi 74184833 430 LGVLAQLIWSRALGFPLERPKSMSTDGL 457
Cdd:cd06106 401 LGPLTQLVWDRILGLPIERPKSLSLEGL 428
PRK09569 PRK09569
citrate (Si)-synthase;
33-464 0e+00

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 609.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   33 LKDVLSNLIPKEQARIKTFKQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGE 112
Cdd:PRK09569   3 LKETLKQKIEEHRPRTTRLVKEFGSVVIDEVTIEQCIGGARDIRSLVTDISYLDPQEGIRFRGKTIPETFEALPKAPGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  113 EPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEG-MNR 191
Cdd:PRK09569  83 YPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPRDSHPMVMLSVGILAMQRESKFAKFYNEGkFNK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  192 AKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIgAIDSRLDWSHNFTNMLGYtDPQFTELMRLYLTIHSDHEGGNVS 271
Cdd:PRK09569 163 MDAWEYMYEDASDLVARIPVIAAYIYNLKYKGDKQI-PSDPELDYGANFAHMIGQ-PKPYKDVARMYFILHSDHESGNVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  272 AHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEV-GKDVSDEKLRDYIWNTLNSGRVVPGYGHAVL 350
Cdd:PRK09569 241 AHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGWIQQFQEKLgGEEPTKEQVEQALWDTLNAGQVIPGYGHAVL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  351 RKTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPNILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRAL 430
Cdd:PRK09569 321 RKTDPRYTAQREFCLKHLPDDPLFKLVAMIFEVAPGVLTEHGKTKNPWPNVDAQSGVIQWYYGVKEWDFYTVLFGVGRAL 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 74184833  431 GVLAQLIWSRALGFPLERPKSMSTDGLMKFVDSK 464
Cdd:PRK09569 401 GVMANITWDRGLGYAIERPKSVTTEMLEKWAAEG 434
PLN02456 PLN02456
citrate synthase
29-454 0e+00

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 529.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   29 SSTNLKDVLSNLIPKEQARIKtfKQQHGKTVVGQITVDmmyGGMRGMKGLVYETSVLDPDEGI-RFRGYSIPECQKMLPK 107
Cdd:PLN02456  30 TGKDYESPLSELGPVQAERLK--KIKAGKDDLGLKTVD---PGYRNTAPVLSEISLIDGDEGIlRFRGYPIEELAEKSPF 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  108 akggeeplpEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAE 187
Cdd:PLN02456 105 ---------EEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVSGVMALSTFSPDANAYLR 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  188 GMNRAKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIGaiDSRLDWSHNFTNMLGY-------TDPQFTELMRLYLT 260
Cdd:PLN02456 176 GQHKYKSWEVRDEDIVRLIGKLPTLAAAIYRRMYGRGPVIP--DNSLDYAENFLYMLGSlgdrsykPDPRLARLLDLYFI 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  261 IHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLtqlqKEVGkdvSDEKLRDYIWNTLNSGR 340
Cdd:PLN02456 254 IHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKML----KEIG---TVENIPEYVEGVKNSKK 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  341 VVPGYGHAVLRKTDPRYSCQREFAL---KHLPKDPMFKLVAQLYKIVpnILLEQGKAKNPWPNVDAHSGVLLQYYGMTEm 417
Cdd:PLN02456 327 VLPGFGHRVYKNYDPRAKCIREFALevfKHVGDDPLFKVASALEEVA--LLDEYFKVRKLYPNVDFYSGVLLRALGFPE- 403
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 74184833  418 NYYTVLFGVSRALGVLAQliWSRALGFPLER---PKSMST 454
Cdd:PLN02456 404 EFFTVLFAVSRAAGYLSQ--WDEALGLPDERimrPKQVYT 441
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
70-453 4.24e-149

Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism.


Pssm-ID: 99871 [Multi-domain]  Cd Length: 358  Bit Score: 428.94  E-value: 4.24e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  70 GGMRGMKGLVYETSVLDPDEGI-RFRGYSIPECQKMlpkakggeePLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALP 148
Cdd:cd06118   1 PGLEGVKAKETSISYIDGDEGIlRYRGYDIEELAEK---------SSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 149 SHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAyaegmnraKYWELIYEDCMDLIAKLPCVAAKIYRnlYREGSSIG 228
Cdd:cd06118  72 EHVVEILDLLPKNAHPMDVLRTAVSALGSFDPFARD--------KSPEARYEKAIRLIAKLPTIAANIYR--NREGLEII 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 229 AIDSRLDWSHNFTNMLGY--TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 306
Cdd:cd06118 142 APDPDLSYAENFLYMLFGeePDPEEAKAMDLALILHADHEG-NASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANE 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 307 EVLVWLTQLQKEvgkdvsdEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPK---DPMFKLVAQLYKI 383
Cdd:cd06118 221 AVLKMLLEIGTP-------ENVEAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEkgdDKLFEIAEELEEI 293
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 384 VPNILLEqgkaKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMS 453
Cdd:cd06118 294 ALEVLGE----KGIYPNVDFYSGVVYKALGF-PTELFTPLFAVSRAVGWLAHIIEYRENNQRLIRPRAEY 358
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
71-450 7.29e-130

Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.


Pssm-ID: 459747 [Multi-domain]  Cd Length: 357  Bit Score: 379.93  E-value: 7.29e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833    71 GMRGMKGLVYETSVLDPDEG-IRFRGYSIPE-CQKMLPkakggeeplpEGLFWLLVTGQMPTEEQVSWLSREWAKRAALP 148
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGiLRYRGYDIEElAERSSF----------EEVAYLLLTGELPTKEELEEFSAELAAHRELP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   149 SHVVTMLDNFPTNLHPMSQLSAAITALNSESNFArayaeGMNRAKYWELIYEDcmDLIAKLPCVAAKIYRnlYREGSSIG 228
Cdd:pfam00285  71 EDVLELLRALPRDAHPMAVLRAAVSALAAFDPEA-----ISDKADYWENALRD--DLIAKLPTIAAYIYR--HRRGLPPI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   229 AIDSRLDWSHNFTNML-GYT-DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 306
Cdd:pfam00285 142 YPDPDLSYAENFLYMLfGYEpDPEEARALDLYLILHADHEG-NASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   307 EVLVWLTQLQKEvgkdvsdEKLRDYIWNTLNSG-RVVPGYGHAVLRKTDPRYSCQREFALKHLPK---DPMFKLVAQLYK 382
Cdd:pfam00285 221 AVLEMLEEIGSP-------DEVEEYIRKVLNKGkERIMGFGHRVYKNYDPRAKILKEFAEELAEEggdDPLLELAEELEE 293
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74184833   383 IVPNILLEQGkaKNPWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQLIWSRALGfPLERPK 450
Cdd:pfam00285 294 VAPEDLYFVE--KNLYPNVDFYSGVLYHALGIPT-DMFTPLFAISRTAGWLAHWIEQLADN-RIIRPR 357
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
62-451 2.04e-103

Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440141 [Multi-domain]  Cd Length: 387  Bit Score: 313.57  E-value: 2.04e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  62 QITVDMMYGGMRGMKG-LVYETSV--LDPDEGI-RFRGYSIPECQkmlpkakggEEPLPEGLFWLLVTGQMPTEEQVSWL 137
Cdd:COG0372   4 EIDIRAKFTVDPGLEGvVAGETAIsyIDGEKGIlRYRGYPIEDLA---------EKSSFEEVAYLLLYGELPTKEELAEF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 138 SREWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALnseSNFaraYAEGMNRAKywELIYEDCMDLIAKLPCVAAKIY 217
Cdd:COG0372  75 KAELARHRELPEEVKEFLDGFPRDAHPMDVLRTAVSAL---GAF---DPDADDIDP--EARLEKAIRLIAKLPTIAAYAY 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 218 RnlYREGSSIGAIDSRLDWSHNFTNMLGYT--DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNG 295
Cdd:COG0372 147 R--YRRGLPPVYPDPDLSYAENFLYMLFGEepDPEEARALDLLLILHADHEQ-NASTFTARVVASTLADLYSAIAAAIGA 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 296 LAGPLHGLANQEVLVWLtqlqKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHLPKDP 372
Cdd:COG0372 224 LKGPLHGGANEAVLEML----EEIG---SPDNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAeelLEELGDDP 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 373 MFKLVAQLYKIVPNilLEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRAlGFPLERPKS 451
Cdd:COG0372 297 LLEIAEELEEVALE--DEYFIEKKLYPNVDFYSGIVYHALGIpTDM--FTPIFAISRVAGWIAHWLEQRA-DNRIIRPRQ 371
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
70-453 2.05e-97

Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and form homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. This subgroup includes both gram-positive and gram-negative bacteria.


Pssm-ID: 99855 [Multi-domain]  Cd Length: 265  Bit Score: 293.84  E-value: 2.05e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  70 GGMRGMKGLVYETSVLDPDEGI-RFRGYSIPECQKMlpkakggeePLPEGLFWLLVTGQMPteeqvswlsrewakraalp 148
Cdd:cd06101   1 PGLRGVAALESEISVIDGDEGGlRYRGYPIEELAEN---------SSFEEVAYLLLTGELP------------------- 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 149 shvvtmldnfptnlhpmsqlsaaitalnsesnfarayaegmnrakyweliyedcmdliaklpcvaakiyrnlyregssig 228
Cdd:cd06101     --------------------------------------------------------------------------------
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 229 aidsrlDWSHNFTNMLGY--TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 306
Cdd:cd06101  53 ------SYAENFLYMLGGeePDPEFAKAMDLALILHADHEG-NASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANE 125
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 307 EVLVWLTQLQKEVgkdvsDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPK---DPMFKLVAQLYKI 383
Cdd:cd06101 126 AVLKMLEEIGTPK-----NEPAEAYIRKKLNSKRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEkglDPMFELAAELEKI 200
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 384 VPNILLEqgkaKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMS 453
Cdd:cd06101 201 APEVLYE----KKLYPNVDFYSGVLYKAMGFP-TELFTPLFAVSRAVGWLAHLIEQREDGQRIIRPRAEY 265
CS_ACL-C_CCL cd06099
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
235-453 2.21e-89

Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase (ACL) and the C-terminal portion of the large subunit of the two-subunit type ACL. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) from citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. Some CS proteins function as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. CCL cleaves citryl-CoA (CiCoA) to AcCoA and OAA. ACLs catalyze an ATP- and a CoA- dependant cleavage of citrate to form AcCoA and OAA; they do this in a multistep reaction, the final step of which is likely to involve the cleavage of CiCoA to generate AcCoA and OAA. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate CiCoA, and c) the hydrolysis of CiCoA to produce citrate and CoA. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. In fungi, yeast, plants, and animals ACL is cytosolic and generates AcCoA for lipogenesis. In several groups of autotrophic prokaryotes and archaea, ACL carries out the citrate-cleavage reaction of the reductive tricarboxylic acid (rTCA) cycle. In the family Aquificaceae this latter reaction in the rTCA cycle is carried out via a two enzyme system the second enzyme of which is CCL.


Pssm-ID: 99853 [Multi-domain]  Cd Length: 213  Bit Score: 271.13  E-value: 2.21e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 235 DWSHNFTNMLGY--TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWL 312
Cdd:cd06099   1 SYAENFLYMLGGeePDPEFARAMDLALILHADHEG-NASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAVLKML 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 313 TQLQKEVgkdvsDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPK---DPMFKLVAQLYKIVPNILL 389
Cdd:cd06099  80 EEIGTPK-----NEPAEAYIRKKLESKRVIMGFGHRVYKKYDPRATVLKKFAEELLKEdgdDPMFELAAELEKIAEEVLY 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74184833 390 EqgkaKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMS 453
Cdd:cd06099 155 E----KKLYPNVDFYSGVLYKAMGFP-TELFTPLFAVARAVGWLAHLIEQLEDNFKIIRPRSEY 213
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
83-454 3.03e-47

Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs, including EcCS, are strongly and specifically inhibited by NADH through an allosteric mechanism. Included in this group is an NADH-insensitive type II Acetobacter acetii CS which has retained many of the residues used by EcCS for NADH binding. C. aurantiacus is a gram-negative thermophilic green gliding bacterium; its CS belonging to this group may be a type I CS. It is not inhibited by NADH or 2-oxoglutarate and is inhibited by ATP. Both gram-positive and gram-negative bacteria are found in this group. This group also contains three Arabidopsis peroxisomal CS proteins, CYS-1, -2, and -3 which participate in the glyoxylate cycle. AthCYS1, in addition to a peroxisomal targeting sequence, has a predicted secretory signal peptide; it may be targeted to both the secretory pathway and the peroxisomes and perhaps is located in the extracellular matrix. AthCSY1 is expressed only in siliques and specifically in developing seeds. AthCSY2 and 3 are active during seed germination and seedling development and are thought to participate in the beta-oxidation of fatty acids.


Pssm-ID: 99860  Cd Length: 382  Bit Score: 167.23  E-value: 3.03e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  83 SVLDPDEGI-RFRGYSIPEcqkmLPKAKGGEEPLpeglfWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTN 161
Cdd:cd06107  20 TYIDGDKGIlLYRGYPIEQ----LAESSTYEEVA-----YLLLWGELPTQEQYDEFQRRLSEHMMVPESVHRLIQTFPRD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 162 LHPMSQLSAAITALNS---ESNFARAYAEGMNRAkywELIYEDCMDLIAKLPCVAAKIYRnlYREGSSIGAIDSRLDWSH 238
Cdd:cd06107  91 AHPMGILCAGLSALSAfypEAIPAHTGDLYQNNP---EVRDKQIIRTLAKMPTIAAAAYC--HRIGRPFVYPRANLSYIE 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 239 NFTNMLGYTD-------PQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVW 311
Cdd:cd06107 166 NFLYMMGYVDqepyepnPRLARALDRLWILHADHEM-NCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEAALKM 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 312 LtqlqKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHLPKDPMFKLVAQLYKIVPNIl 388
Cdd:cd06107 245 L----REIG---TPENVPAFIERVKNGKRRLMGFGHRVYKNYDPRAKVIREILhevLTEVEKDPLLKVAMELERIALED- 316
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74184833 389 lEQGKAKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQliWSRALGFPLE---RPKSMST 454
Cdd:cd06107 317 -EYFVSRKLYPNVDFYSGFIYKALGF-PPEFFTVLFAVARTSGWMAH--WREMMEDPLQriwRPRQVYT 381
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
83-443 2.22e-46

Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism.


Pssm-ID: 99865  Cd Length: 373  Bit Score: 164.90  E-value: 2.22e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  83 SVLDPDEGI-RFRGYSIPEcqkmLPKAKGGEEplpegLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTN 161
Cdd:cd06112  16 SYIDGKNGIlEYRGYDIEE----LAEYSSFEE-----VALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMMKCFPET 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 162 LHPMSQLSAAITALNSesNFARAYAEGMNRAKywelIYEDCMDLIAKLPCVAAKIYRnlYREGSSIgaIDSRLDWSH--N 239
Cdd:cd06112  87 GHPMDMLQATVAALGM--FYPKPEVLKPNPDY----IDAATVKLIAKMPTLVAMWAR--IRNGDDP--IEPRPDLDYaeN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 240 FTNML--GYTDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLtqlqK 317
Cdd:cd06112 157 FLYMLfgEEPDPATAKILDACLILHAEHTM-NASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEML----E 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 318 EVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFAlKHLPK-----DPMFKLVAQLYKIVPNILLEQG 392
Cdd:cd06112 232 EIG---SPENVKAYLDKKLANKQKIWGFGHRVYKTKDPRATILQKLA-EDLFAkmgelSKLYEIALEVERLCEELLGHKG 307
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 74184833 393 KaknpWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQliWSRALG 443
Cdd:cd06112 308 V----YPNVDFYSGIVYKELGIPA-DLFTPIFAVARVAGWLAH--WKEQLG 351
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
73-437 4.30e-44

Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains proteins similar to BsCS-II, the major CS of the gram-positive bacterium Bacillus subtilis. A mutation in the gene which encodes BsCS-II (citZ gene) has been described which resulted in a significant loss of CS activity, partial glutamate auxotrophy, and a sporulation deficiency, all of which are characteristic of strains defective in the Krebs cycle. Streptococcus mutans CS, found in this group, may participate in a pathway for the anaerobic biosynthesis of glutamate. This group also contains functionally uncharacterized CSs of various gram-negative bacteria. Some of the gram-negative species represented in this group have a second CS isozyme found in another group. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


Pssm-ID: 99863 [Multi-domain]  Cd Length: 356  Bit Score: 158.21  E-value: 4.30e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  73 RGMKGLVYETSVL---DPDEGI-RFRGYSIPEcqkmLPKAKGGEEPLpeglfWLLVTGQMPTEEQVSWLSREWAKRAALP 148
Cdd:cd06110   1 KGLEGVIAADSKIsyiDGDAGIlIYRGYDIHD----LAENSTFEEVA-----YLLWNGELPTAEELDAFKAQLAAERELP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 149 SHVVTMLDNFPTNLHPMSQLSAAITAL---NSEsnfarayAEGMNRakywELIYEDCMDLIAKLPCVAAKIYRnlYREGS 225
Cdd:cd06110  72 AEIIDLLKLLPKDAHPMDVLRTAVSALalyDPE-------ADDMSR----EANLRKAIRLIAKMPTIVAAFHR--IRNGL 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 226 SIGAIDSRLDWSHNFTNMLGYT--DPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGL 303
Cdd:cd06110 139 EPVAPDPDLSHAANFLYMLTGEkpSEEAARAFDVALILHADHEL-NASTFAARVVASTLSDMYSAVTAAIGALKGPLHGG 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 304 ANQEVLVWLTqlqkEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKhLPKD----PMFKLVAQ 379
Cdd:cd06110 218 ANERVMKMLL----EIG---SVDNVAAYVKDKLANKEKIMGFGHRVYKTGDPRAKHLREMSRR-LGKEtgepKWYEMSEA 289
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 74184833 380 LYKIVPNilleqgkAKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQLI 437
Cdd:cd06110 290 IEQAMRD-------EKGLNPNVDFYSASVYYMLGI-PVDLFTPIFAISRVSGWCAHIL 339
AthCS_per_like cd06115
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ...
83-445 4.87e-38

Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains three Arabidopsis peroxisomal CS proteins, CYS1, -2, and -3 which are involved in the glyoxylate cycle. AthCYS1, in addition to a peroxisomal targeting sequence, has a predicted secretory signal peptide; it may be targeted to both the secretory pathway and the peroxisomes and is thought to be located in the extracellular matrix. AthCSY1 is expressed only in siliques and specifically in developing seeds. AthCSY2 and 3 are active during seed germination and seedling development and are thought to participate in the beta-oxidation of fatty acids.


Pssm-ID: 99868  Cd Length: 410  Bit Score: 142.96  E-value: 4.87e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  83 SVLDPDEGI-RFRGYSIPEcqkMLPKAKGGEeplpegLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTN 161
Cdd:cd06115  40 SYIDGDKGIlRYRGYPIEE---LAEKSTFLE------VAYLLIYGNLPTKSQLSDWEFAVSQHTAVPTGVLDMIKSFPHD 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 162 LHPMSQLSAAITALNS---ESNFARAyaeGMNRAKYWELIYEDCMDLIAKLPCVAAKIYRNlyREGSSIGAIDSRLDWSH 238
Cdd:cd06115 111 AHPMGMLVSAISALSAfhpEANPALA---GQDIYKNKQVRDKQIVRILGKAPTIAAAAYRR--RAGRPPNLPSQDLSYTE 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 239 NFTNML---GYTD----PQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVW 311
Cdd:cd06115 186 NFLYMLdslGERKykpnPRLARALDILFILHAEHEM-NCSTAAVRHLASSGVDVYTAVAGAVGALYGPLHGGANEAVLRM 264
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 312 LTqlqkEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHLPKDPMFKLVAQLYKIVpnIL 388
Cdd:cd06115 265 LA----EIG---TVENIPAFIEGVKNRKRKLSGFGHRVYKNYDPRAKIIKKLAdevFEIVGKDPLIEIAVALEKAA--LS 335
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 74184833 389 LEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQliWSRALGFP 445
Cdd:cd06115 336 DEYFVKRKLYPNVDFYSGLIYRAMGFpTDF--FPVLFAIPRMAGYLAH--WRESLDDP 389
gltA PRK05614
citrate synthase;
85-436 9.35e-38

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 142.32  E-value: 9.35e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   85 LDPDEGI-RFRGYSIpecqkmlpkakggeEPLPE-GLF----WLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNF 158
Cdd:PRK05614  62 IDGDKGIlLYRGYPI--------------EQLAEkSDFlevcYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGF 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  159 PTNLHPMSQLSAAITALnseSNFarayaegmnrakyweliYEDCMD-------------LIAKLPCVAAKIYRnlYREGS 225
Cdd:PRK05614 128 RRDAHPMAVLCGVVGAL---SAF-----------------YHDSLDindpehreiaairLIAKMPTLAAMAYK--YSIGQ 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  226 SIGAIDSRLDWSHNFTNML-GY------TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAG 298
Cdd:PRK05614 186 PFVYPRNDLSYAENFLRMMfATpceeyeVNPVLVRALDRIFILHADHEQ-NASTSTVRLAGSSGANPFACIAAGIAALWG 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  299 PLHGLANQEVLVWLtqlqKEVGkdvSDEKLRDYIWNTL--NSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHL-PKDP 372
Cdd:PRK05614 265 PAHGGANEAVLKML----EEIG---SVDNIPEFIARAKdkNDGFRLMGFGHRVYKNYDPRAKIMRETChevLKELgLNDP 337
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74184833  373 MFKLVAQLYKIVPNIllEQGKAKNPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQL 436
Cdd:PRK05614 338 LLEVAMELEEIALND--EYFIERKLYPNVDFYSGIILKALGIpTSM--FTVIFALARTVGWIAHW 398
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
85-454 1.14e-36

Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). This group is similar to gram-negative Escherichia coli (Ec) CS (type II, gltA) and Arabidopsis thaliana (Ath) peroxisomal (Per) CS. However EcCS and AthPerCS are not found in this group. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. C. aurantiacus is a gram-negative thermophilic green gliding bacterium, its CS belonging to this group may be a type I CS; it is not inhibited by NADH or 2-oxoglutarate and is inhibited by ATP. Both gram-positive and gram-negative bacteria are found in this group.


Pssm-ID: 99869  Cd Length: 384  Bit Score: 138.81  E-value: 1.14e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  85 LDPDEGI-RFRGYSIPECqkmlpkakgGEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLH 163
Cdd:cd06116  22 IDGEKGIlRYRGYPIEQL---------AEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENLKKFMDGFRYDAH 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 164 PMSQLSAAITALNSESNFARAYAEGMNRAKyweliyeDCMDLIAKLPCVAAKIYRnlYREGSSIGAIDSRLDWSHNFTNM 243
Cdd:cd06116  93 PMGILISSVAALSTFYPEAKNIGDEEQRNK-------QIIRLIGKMPTIAAFAYR--HRLGLPYVLPDNDLSYTGNFLSM 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 244 LGY-------TDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLtqlq 316
Cdd:cd06116 164 LFKmtepkyePNPVLAKALDVLFILHADHEQ-NCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRML---- 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 317 KEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHLPKDPMFKLVAQLYKIVpnILLEQGK 393
Cdd:cd06116 239 QQIG---SPKNIPDFIETVKQGKERLMGFGHRVYKNYDPRARIIKKIAdevFEATGRNPLLDIAVELEKIA--LEDEYFI 313
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74184833 394 AKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQliWSRALGFP---LERPKSMST 454
Cdd:cd06116 314 SRKLYPNVDFYSGLIYQALGFP-TEAFTVLFAIPRTSGWLAQ--WIEMLRDPeqkIARPRQVYT 374
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
87-437 2.16e-35

Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) a carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) hydrolysis of citryl-CoA to produce citrate and CoA. CSs are found in two structural types: type I (homodimeric) and type II CSs (homohexameric). Type II CSs are unique to gram-negative bacteria. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria. Type I CS is active as a homodimer, both subunits participating in the active site. Type II CS is a hexamer of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. This subgroup includes both gram-positive and gram-negative bacteria.


Pssm-ID: 99866  Cd Length: 406  Bit Score: 135.86  E-value: 2.16e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  87 PDEG-IRFRGYSIPECQKMLPKAK--GGEEplpegLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVV-TMLDNFPTNl 162
Cdd:cd06113  33 PCPGkLYYRGYDVEDLVNGAQKENrfGFEE-----TAYLLLFGYLPNKEELEEFCEILSSYRTLPDNFVeDVILKAPSK- 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 163 HPMSQLSAAITALNSesnfaraY---AEGMNRakywELIYEDCMDLIAKLPCVAAKIYR--NLYREGSS--IGAIDSRLD 235
Cdd:cd06113 107 DIMNKLQRSVLALYS-------YddkPDDISL----ENVLRQSIQLIARLPTIAVYAYQakRHYYDGESlyIHHPQPELS 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 236 WSHNFTNMLgYTDPQFTE----LMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVW 311
Cdd:cd06113 176 TAENILSML-RPDKKYTEleakLLDLCLVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEM 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 312 LTQLQKEVgKDVSDEK-LRDYIWNTLN------SGrVVPGYGHAVLRKTDPRYSCQREFAlKHLPK----DPMFKLVAQL 380
Cdd:cd06113 255 LEDIKENV-KDWTDEDeVRAYLRKILNkeafdkSG-LIYGMGHAVYTLSDPRAVVLKKYA-RSLAKekgrEEEFALYERI 331
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74184833 381 YKIVPNILLEQ-GKAKNPWPNVDAHSGVLlqyYGM----TEMnyYTVLFGVSRALGVLAQLI 437
Cdd:cd06113 332 ERLAPEVIAEErGIGKTVCANVDFYSGFV---YKMlgipQEL--YTPLFAVARIVGWCAHRI 388
PRK14036 PRK14036
citrate synthase; Provisional
83-443 2.45e-35

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 135.09  E-value: 2.45e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   83 SVLDPDEGI-RFRGYSIPEcqkmLPKAKGGEEPLpeglfWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTN 161
Cdd:PRK14036  19 SYVDGQKGIlEYRGYPIEE----LAEKSSFLETA-----YLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMMKCFPET 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  162 LHPMSQLSAAITALNSesNFARAyaeGMNRAKYwelIYEDCMDLIAKLPC-VAAkiyRNLYREGSSigAIDSR--LDWSH 238
Cdd:PRK14036  90 GHPMDALQASAAALGL--FYSRR---ALDDPEY---IRDAVVRLIAKIPTmVAA---FQLIRKGND--PIQPRddLDYAA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  239 NFTNMLG--YTDPQFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLtqlq 316
Cdd:PRK14036 157 NFLYMLTerEPDPLAARIFDRCLILHAEHTI-NASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAML---- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  317 KEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA---LKHLPKDPMFKLVAQLYKIVPNILLEQGK 393
Cdd:PRK14036 232 EEIG---SVENVRPYLDERLANKQKIMGFGHREYKVKDPRATILQKLAeelFARFGHDEYYEIALELERVAEERLGPKGI 308
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 74184833  394 aknpWPNVDAHSGVLLQYYGMTEmNYYTVLFGVSRALGVLAQliWSRALG 443
Cdd:PRK14036 309 ----YPNVDFYSGLVYRKLGIPR-DLFTPIFAIARVAGWLAH--WREQLG 351
PRK14032 PRK14032
citrate synthase; Provisional
87-434 4.39e-33

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 130.02  E-value: 4.39e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   87 PDEG-IRFRGYSIPECQKMLPKAK--GGEEplpegLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVV--TMLDNFPTN 161
Cdd:PRK14032  63 PDEGkLYYRGYDIKDLVNGFLKEKrfGFEE-----VAYLLLFGELPTKEELAEFTELLGDYRELPDGFTrdMILKAPSKD 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  162 LhpMSQLSAAITALNSesnfaraYAEGMNRAKYWELIyEDCMDLIAKLPCVAAKIYR--NLYREGSS--IGAIDSRLDWS 237
Cdd:PRK14032 138 I--MNSLARSVLALYS-------YDDNPDDTSIDNVL-RQSISLIARFPTLAVYAYQayRHYHDGKSlyIHPPKPELSTA 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  238 HNFTNMLgYTDPQFTEL----MRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLT 313
Cdd:PRK14032 208 ENILYML-RPDNKYTELearlLDLALVLHAEHGGGNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFE 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  314 QLQKEVGKDVSDEKLRDYIWNTLN------SGRVVpGYGHAVLRKTDPRYSCQREFAL-----KHLPKDpmFKLVAQLYK 382
Cdd:PRK14032 287 DIKENVKDWEDEDEIADYLTKILNkeafdkSGLIY-GMGHAVYTISDPRAVILKKFAEklakeKGREEE--FNLYEKIEK 363
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 74184833  383 IVPNILLEQ-GKAKNPWPNVDAHSGVLlqyYGM----TEMnyYTVLFGVSRALGVLA 434
Cdd:PRK14032 364 LAPELIAEErGIYKGVSANVDFYSGFV---YDMlgipEEL--YTPLFAIARIVGWSA 415
PRK14034 PRK14034
citrate synthase; Provisional
73-437 6.04e-31

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 122.57  E-value: 6.04e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   73 RGMKGLVYETSVLDP--DEGIRFRGYSIPECqkmlpkakgGEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSH 150
Cdd:PRK14034   5 RGLEGVVATTSSVSSiiDDTLTYVGYNIDDL---------AENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  151 VVTMLDNFPTN-LHPMSQLSAAITALNSESNFARAYAEGMNRAKyweliyedCMDLIAKLPCVAAKIYRnlYREGSSIGA 229
Cdd:PRK14034  76 IIEHLKQYDLKkVHPMSVLRTAISMLGLYDEEAEIMDEEANYRK--------AVRLQAKVPTIVAAFSR--IRKGLDPVE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  230 IDSRLDWSHNFTNMLGYTDPQFTEL--MRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQE 307
Cdd:PRK14034 146 PRKDLSLAANFLYMLNGEEPDEVEVeaFNKALVLHADHEL-NASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANEN 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  308 VLVWLTQLQKEvgkdvsdEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFA--LKHLPKDPM-FKLVAQLYKIV 384
Cdd:PRK14034 225 VMKMLTEIGEE-------ENVESYIHNKLQNKEKIMGFGHRVYRQGDPRAKHLREMSkrLTVLLGEEKwYNMSIKIEEIV 297
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 74184833  385 PNilleqgkAKNPWPNVDAHSGVLLQYYGMtEMNYYTVLFGVSRALGVLAQLI 437
Cdd:PRK14034 298 TK-------EKGLPPNVDFYSASVYHCLGI-DHDLFTPIFAISRMSGWLAHIL 342
PRK14035 PRK14035
citrate synthase; Provisional
73-436 4.58e-27

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 111.77  E-value: 4.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   73 RGMKGLVY-ETSVLD-PDEGIRFRGYSIPECQkmlpkakggEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSH 150
Cdd:PRK14035   5 RGLEGVIAaETKISSiIDSQLTYAGYDIDDLA---------ENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  151 VVTMLDNFPT-NLHPMSQLSAAITALNSESNFARAYAEgmnrakywELIYEDCMDLIAKLPCVAAKIYRnlYREGSSIGA 229
Cdd:PRK14035  76 VYQHFEEYSTdHVHPMTALRTSVSYLAHFDPDAEEESD--------EARYERAIRIQAKVASLVTAFAR--VRQGKEPLK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  230 IDSRLDWSHNFTNMLGYTDPQFTEL--MRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQE 307
Cdd:PRK14035 146 PRPDLSYAANFLYMLRGELPTDIEVeaFNKALVLHADHEL-NASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANER 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  308 VLVWLTQLqKEVGkDVSdeklrDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFAlKHLPKDPMFKlvaQLYKIVPNI 387
Cdd:PRK14035 225 VMDMLSEI-RSIG-DVD-----AYLDEKFANKEKIMGFGHRVYKDGDPRAKYLREMS-RKITKGTGRE---ELFEMSVKI 293
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 74184833  388 LLEQGKAKNPWPNVDAHSGVLlqYYGM-TEMNYYTVLFGVSRALGVLAQL 436
Cdd:PRK14035 294 EKRMKEEKGLIPNVDFYSATV--YHVMgIPHDLFTPIFAVSRVAGWIAHI 341
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
117-441 4.94e-27

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 111.58  E-value: 4.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  117 EGLFWLLVTGQMPTEEQVSWLS-REWAKRAALPShVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGMNRAKyw 195
Cdd:PRK14033  50 EEVAYLLWNGELPTDAELALFSqRERAYRRLDRS-VLSLIDKLPTTCHPMDVVRTAVSYLGAEDPEADDSSPEANLAK-- 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  196 eliyedCMDLIAKLPCVAAKIYRNlyREGSSIGAIDSRLDWSHNFTNM-LG-YTDPQFTELMRLYLTIHSDHeGGNVSAH 273
Cdd:PRK14033 127 ------ALRLFAVLPTIVAADQRR--RRGLDPIAPRSDLGYAENFLHMcFGeVPEPEVVRAFEVSLILYAEH-SFNASTF 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  274 TSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLvwltQLQKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKT 353
Cdd:PRK14033 198 TARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVM----HTMLEIG---DPARAAEWLRDALARKEKVMGFGHRVYKHG 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  354 DPRYSCQREfALKHLPKDPMFKLVAQLYKIvpnilLEQG--KAKNPWPNVDAHSGVLlqYYGM---TEMnyYTVLFGVSR 428
Cdd:PRK14033 271 DSRVPTMKA-ALRRVAAVRDGQRWLDIYEA-----LEKAmaEATGIKPNLDFPAGPA--YYLMgfdIDF--FTPIFVMSR 340
                        330
                 ....*....|...
gi 74184833  429 ALGVLAQLIWSRA 441
Cdd:PRK14033 341 ITGWTAHIMEQRA 353
PRK12349 PRK12349
citrate synthase;
74-437 9.21e-26

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 107.88  E-value: 9.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   74 GMKGLVY-ET--SVLDPDEG-IRFRGYSIPEcqkmLPKAKGGEEplpegLFWLLVTGQMPTEEQVSWLSREWAKRAALPS 149
Cdd:PRK12349   8 GLDGVIAaETkiSFLDTVKGeIVIQGYDLIE----LSKTKEYLD-----IVHLLLEEHLPNEDEKATLEKKLKEEYAVPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  150 HVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGMNRAKyweliyedCMDLIAKLPCVAAKIYRNLyrEGSSIGA 229
Cdd:PRK12349  79 GVFNILKALPKETHPMDGLRTGVSALAGYDNDIEDRSLEVNKSR--------AYKLLSKVPNIVANSYHIL--NNEEPIE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  230 IDSRLDWSHNFTNMLGYTDP--QFTELMRLYLTIHSDHEGGNvSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQE 307
Cdd:PRK12349 149 PLKELSYSANFLYMLTGKKPteLEEKIFDRSLVLYSEHEMPN-STFTARVIASTQSDLYGALTGAVASLKGSLHGGANEA 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  308 VLVWLTQlqkevGKDVSD-EKLrdyIWNTLNSGRVVPGYGHAV-LRKTDPRYSCQREfALKHL-PKDPMFKLVAqlykiv 384
Cdd:PRK12349 228 VMYMLLE-----AGTVEKfEEL---LQKKLYNKEKIMGFGHRVyMKKMDPRALMMKE-ALKQLcDVKGDYTLYE------ 292
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 74184833  385 pniLLEQG-----KAKNPWPNVDAHSGVLLQYYGMTeMNYYTVLFGVSRALGVLAQLI 437
Cdd:PRK12349 293 ---MCEAGekimeKEKGLYPNLDYYAAPVYWMLGIP-IQLYTPIFFSSRTVGLCAHVI 346
PRK14037 PRK14037
citrate synthase; Provisional
85-437 2.75e-23

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 100.98  E-value: 2.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833   85 LDPDEGI-RFRGYSIPEcqkmLPKAKGGEEplpegLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLH 163
Cdd:PRK14037  21 IDGEKGIlRYRGYNIED----LVNYGSYEE-----TIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  164 PMSQLSAAITALNS-ESNFarayaegmnraKYWELIYEDCMDLIAKLPCVAAKIYRnlYREGSSIGAIDSRLDWSHNFTN 242
Cdd:PRK14037  92 AIGLMEAAFAALASiDKNF-----------KWKENDKEKAISIIAKMATIVANVYR--RKEGNKPRIPEPSDSFAESFLL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  243 MLGYTDPQFTEL--MRLYLTIHSDHEggnVSAHTSH-LVG-SALSDPYLSFAAAMNGLAGPLHGLANQEVLvwlTQLQkE 318
Cdd:PRK14037 159 ASFAREPTAEEIkaMDAALILYTDHE---VPASTTAaLVAaSTLSDMYSCITAALAALKGPLHGGAAEEAF---KQFV-E 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  319 VGK-DVSDEKLRDyiwNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPNILLEQGKAKNP 397
Cdd:PRK14037 232 IGDpNNVEMWFND---KIINGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSEAKKYFEIAQKLEELGIKQFGSKGI 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 74184833  398 WPNVDAHSGVLlqYYGMT-EMNYYTVLFGVSRALGVLAQLI 437
Cdd:PRK14037 309 YPNTDFYSGIV--FYALGfPVYMFTALFALSRTLGWLAHII 347
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
90-441 5.40e-20

Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and oxalacetate (OAA) to form 2-methylcitrate and coenzyme A (CoA) during propionate metabolism. Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and OAA to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). This group contains proteins similar to the E. coli 2MCS, EcPrpC. EcPrpC is one of two CS isozymes in the gram-negative E. coli. EcPrpC is a dimeric (type I ) CS; it is induced during growth on propionate and prefers PrCoA as a substrate though it has partial CS activity with AcCoA. This group also includes Salmonella typhimurium PrpC and Ralstonia eutropha (Re) 2-MCS1 which are also induced during growth on propionate and prefer PrCoA as substrate, but can also use AcCoA. Re 2-MCS1 can use butyryl-CoA and valeryl-CoA at a lower rate. A second Ralstonia eutropha 2MCS, Re 2-MCS2, which is induced on propionate is also found in this group. This group may include proteins which may function exclusively as a CS, those which may function exclusively as a 2MCS, or those with dual specificity which functions as both a CS and a 2MCS.


Pssm-ID: 99861 [Multi-domain]  Cd Length: 363  Bit Score: 91.21  E-value: 5.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  90 GIRFRGYSIpecqKMLPKAKGGEEplpegLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQL- 168
Cdd:cd06108  22 GLTYRGYDI----EDLAENATFEE-----VAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPMDVMr 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 169 --SAAITALNSESNFARAYaEGMNRakyweliyedcmdLIAKLPCVAAKIYRnLYREGSSIGAIDSRLDWSHNFTNMLGY 246
Cdd:cd06108  93 tgCSMLGCLEPENEFSQQY-EIAIR-------------LLAIFPSILLYWYH-YSHSGKRIETETDEDSIAGHFLHLLHG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 247 TDP--QFTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQkevgkdvS 324
Cdd:cd06108 158 KKPgeLEIKAMDVSLILYAEHEF-NASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFK-------S 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 325 DEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFAlKHLPKDPMFKLvaqLYKIVPNILLEQGKAKNPWPNVDAH 404
Cdd:cd06108 230 PEEAEQGLLEKLERKELIMGFGHRVYKEGDPRSDIIKKWS-KKLSEEGGDPL---LYQISERIEEVMWEEKKLFPNLDFY 305
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 74184833 405 SGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRA 441
Cdd:cd06108 306 SASAYHFCGIpTEL--FTPIFVMSRVTGWAAHIMEQRA 341
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
73-451 6.35e-19

Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and coenzyme A (CoA) during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains proteins similar to BsCS-I, one of two CS isozymes in the gram-positive B. subtilis. The majority of CS activity in B. subtilis is provided by the other isozyme, BsCS-II (not included in this group). BsCS-I has a lower catalytic activity than BsCS-II, and has a Glu in place of a key catalytic Asp residue. This change is conserved in other members of this group. For E. coli CS (not included in this group), site directed mutagenesis of the key Asp residue to a Glu converts the enzyme into citryl-CoA lyase which cleaves citryl-CoA to AcCoA and OAA. A null mutation in the gene encoding BsCS-I (citA) had little effect on B. subtilis CS activity or on sporulation. However, disruption of the citA gene in a strain null for the gene encoding BsCS-II resulted in a sporulation deficiency, a characteristic of strains defective in the Krebs cycle. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. Many of the gram-negative species represented in this group have a second CS isozyme which is in another group.


Pssm-ID: 99862 [Multi-domain]  Cd Length: 349  Bit Score: 87.75  E-value: 6.35e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  73 RGMKGLV-YETSVLDPD--EG-IRFRGYSIPEcqkmLPKAKGGEEPLpeglfWLLVTGQMPTEEQVSWLSREWAKRAALP 148
Cdd:cd06109   1 PGLEGVVaAETVLSDVDgeAGrLIIRGYSVED----LAGSASFEDVA-----ALLWNGFFPDLPELEEFRAALAAARALP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 149 SHVVTMLDNFpTNLHPMSQLSAAITALNSESNFARAyaegmnrakyweliyedcMDLIAKLPCVAAKIYRnlYREGSSIG 228
Cdd:cd06109  72 DVVAALLPAL-AGLDPMDALRALLALLPDSPDLATA------------------LRLLAAAPVITAALLR--LSRGKQPI 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 229 AIDSRLDWSHNFTNML-GYTDPQ-FTELMRLYLTIHSDHeGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQ 306
Cdd:cd06109 131 APDPSLSHAADYLRMLtGEPPSEaHVRALDAYLVTVADH-GMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPG 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 307 EVLVWLtqlqKEVGkdvSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREfALKHLPKDPMFKLVAQLYKIVPN 386
Cdd:cd06109 210 PVLDML----DAIG---TPENAEAWLREALARGERLMGFGHRVYRVRDPRADVLKA-AAERLGAPDERLEFAEAVEQAAL 281
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74184833 387 ILLEQGKAKNP-WPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRALGfPLERPKS 451
Cdd:cd06109 282 ALLREYKPGRPlETNVEFYTALLLEALGLpREA--FTPTFAAGRTAGWTAHVLEQARTG-RLIRPQS 345
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
91-440 8.98e-15

Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and oxalacetate (OAA) to form 2-methylcitrate and coenzyme A (CoA) during propionate metabolism. Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and OAA to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). This group contains proteins similar to the E. coli 2MCS, EcPrpC. EcPrpC is one of two CS isozymes in the gram-negative E. coli. EcPrpC is a dimeric (type I ) CS; it is induced during growth on propionate and prefers PrCoA as a substrate, but has a partial CS activity with AcCoA. This group also includes Salmonella typhimurium PrpC and Ralstonia eutropha (Re) 2-MCS1 which are also induced during growth on propionate, prefer PrCoA as substrate, but can also can use AcCoA. Re 2-MCS1 at a low rate can use butyryl-CoA and valeryl-CoA. A second Ralstonia eutropha 2MCS is also found in this group, Re 2-MCS2, which is induced on propionate. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.


Pssm-ID: 99870 [Multi-domain]  Cd Length: 366  Bit Score: 75.65  E-value: 8.98e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  91 IRFRGYSIpecqkmLPKAKGGEEplpEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQLSA 170
Cdd:cd06117  23 LHYRGYDI------LDLAEKCEF---EEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAAAHPMDVMRT 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 171 AITALNSesnfARAYAEGMNRAKYweliyEDCMD-LIAKLPCVAAKIY---RNLYR-----EGSSIGAidsrldwshNFT 241
Cdd:cd06117  94 GVSVLGC----VLPEKEDHPVSGA-----RDIADrLMASLGSILLYWYhysHNGKRievetDDDSIGG---------HFL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 242 NMLGYTDPQ--FTELMRLYLTIHSDHEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLvwltQLQKEV 319
Cdd:cd06117 156 HLLHGEKPSesWEKAMHISLILYAEHEF-NASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAF----EIQQRY 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833 320 GKdvSDEKLRDyIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFAlKHLPKDP----MFKLVAQLYKIVPNIlleqgkaK 395
Cdd:cd06117 231 ES--ADEAEAD-IRRRVENKEVVIGFGHPVYTIADPRNQVIKEVA-KQLSKEGgdmkMFDIAERLETVMWEE-------K 299
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 74184833 396 NPWPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSR 440
Cdd:cd06117 300 KMFPNLDWFSAVSYHMMGVpTAM--FTPLFVIARTTGWSAHIIEQR 343
PRK12351 PRK12351
methylcitrate synthase; Provisional
122-441 2.64e-10

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 61.86  E-value: 2.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  122 LLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITAL------NSESNFARAYaegmnrakyw 195
Cdd:PRK12351  54 LLVHGKLPTQAELAAYKTKLKALRGLPAAVKTVLEAIPAAAHPMDVMRTGVSVLgcllpeKEDHNFSGAR---------- 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  196 eliyeDCMD-LIAKLPCVAAKIYR--------NLYREGSSIGAidsrldwsHnFTNMLGYTDPQ--FTELMRLYLTIHSD 264
Cdd:PRK12351 124 -----DIADrLLASLGSILLYWYHyshngrriEVETDDDSIGG--------H-FLHLLHGKKPSesWVKAMHTSLILYAE 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  265 HEGgNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANqEVLVwltQLQKevGKDVSDEKLRDyIWNTLNSGRVVPG 344
Cdd:PRK12351 190 HEF-NASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGAN-EVAF---EIQQ--RYDTPDEAEAD-IRRRVENKEVVIG 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  345 YGHAVLRKTDPRYSCQREFAlKHLPKDPMFKlvaQLYKIVPNILLEQGKAKNPWPNVDAHSGVllQYYGM---TEMnyYT 421
Cdd:PRK12351 262 FGHPVYTISDPRNKVIKEVA-KKLSKEAGDT---KLYDIAERLETVMWEEKKMFPNLDWFSAV--SYHMMgvpTAM--FT 333
                        330       340
                 ....*....|....*....|
gi 74184833  422 VLFGVSRALGVLAQLIWSRA 441
Cdd:PRK12351 334 PLFVISRTTGWAAHVIEQRQ 353
PRK12350 PRK12350
citrate synthase 2; Provisional
231-451 8.49e-10

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 59.98  E-value: 8.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  231 DSRLDWSHNFTNML-----GYTDPQFTELMRLYLTIHSDHeGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLAN 305
Cdd:PRK12350 129 QREIDHAATILERFmgrwrGEPDPAHVAALDAYWVSAAEH-GMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAP 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  306 QEVLVWLTqlqkEVGKDvsdEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREfALKHLPKdPMFKLVAQLYKIVP 385
Cdd:PRK12350 208 ARVLPMLD----AVERT---GDARGWVKGALDRGERLMGFGHRVYRAEDPRARVLRA-TAKRLGA-PRYEVAEAVEQAAL 278
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74184833  386 NILleqgKAKNP----WPNVDAHSGVLLQYYGM-TEMnyYTVLFGVSRALGVLAQLIWSRALGfPLERPKS 451
Cdd:PRK12350 279 AEL----RERRPdrplETNVEFWAAVLLDFAGVpAHM--FTAMFTCGRTAGWSAHILEQKRTG-RLVRPSA 342
PLN02522 PLN02522
ATP citrate (pro-S)-lyase
210-448 2.84e-03

ATP citrate (pro-S)-lyase


Pssm-ID: 178137 [Multi-domain]  Cd Length: 608  Bit Score: 40.19  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  210 PCVAAKIYRNLYREGSSIGAIDSRLdWshnFTNMLgytdPQF-TELMRLYLTIHSDHeGGNVS-AHTSHLVGSALSDPYL 287
Cdd:PLN02522 365 PCYAGVPMSSIIEKDYGVGDVISLL-W---FKRSL----PRYcTKFIEMCIMLCADH-GPCVSgAHNTIVTARAGKDLVS 435
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  288 SFAAAMNGLaGPLHGLANQEVLVWLtqlqkevgKDVSDEKL--RDYIWNTLNSGRVVPGYGHAVLRKT--DPRYSCQREF 363
Cdd:PLN02522 436 SLVSGLLTI-GPRFGGAIDDAARYF--------KDAYDRGLtpYEFVEGMKKKGIRVPGIGHRIKSRDnrDKRVELLQKY 506
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184833  364 ALKHLPKDPMFKLVAQlykiVPNILLEqgKAKNPWPNVDAHSGV----LLQYYGM---------TEMNYYTVLFGVSRAL 430
Cdd:PLN02522 507 ARTHFPSVKYMEYAVQ----VETYTLS--KANNLVLNVDGAIGSlfldLLAGSGMftkqeideiVEIGYLNGLFVLARSI 580
                        250
                 ....*....|....*...
gi 74184833  431 GVLAQLIWSRALGFPLER 448
Cdd:PLN02522 581 GLIGHTFDQKRLKQPLYR 598
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH