|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
489-1094 |
0e+00 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 952.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 489 SATLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPfTGDHKQKFYWGHKEILIPVFKNMADAMKKHPEVDV 568
Cdd:PLN02522 3 TGQLFSRTTQALFYNYKQLPVQRMLDFDFLCGRETPSVAGIINP-GSEGFQKLFFGQEEIAIPVHGSIEAACKAHPTADV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 569 LINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILA 648
Cdd:PLN02522 82 FINFASFRSAAASSMEALKQPTIRVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTLDNIIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 649 SKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIGGTEEYKIC 728
Cdd:PLN02522 162 CKLYRPGSVGFVSKSGGMSNEMYNVIARVTDGIYEGIAIGGDVFPGSTLSDHVLRFNNIPQIKMIVVLGELGGRDEYSLV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 729 RGIKEGRLTKPVVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVAKG 808
Cdd:PLN02522 242 EALKQGKVSKPVVAWVSGTCARLFKSEVQFGHAGAKSGGDMESAQAKNKALKDAGAIVPTSFEALEAAIKETFEKLVEEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 809 AIVPAQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQRRLPKYSCQ 888
Cdd:PLN02522 322 KIIPVKEVTPPQIPEDLNSAIKSGKVRAPTHIVSTISDDRGEEPCYAGVPMSSIIEKDYGVGDVISLLWFKRSLPRYCTK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 889 FIEMCLMVTADHGPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGK 968
Cdd:PLN02522 402 FIEMCIMLCADHGPCVSGAHNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDAYDRGLTPYEFVEGMKKKGI 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 969 LIMGIGHRVKSINNPDMRVQILKDFVKQHFPATPLLDYALEVEKITTSKKPNLILNVDGFIGVAFVDMLRNCGSFTREEA 1048
Cdd:PLN02522 482 RVPGIGHRIKSRDNRDKRVELLQKYARTHFPSVKYMEYAVQVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQEI 561
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 313151222 1049 DEYVDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYV 1094
Cdd:PLN02522 562 DEIVEIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYT 607
|
|
| PLN02235 |
PLN02235 |
ATP citrate (pro-S)-lyase |
1-419 |
8.70e-134 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 177879 [Multi-domain] Cd Length: 423 Bit Score: 412.24 E-value: 8.70e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 1 MSAKAISEQTGKELLYKYICTTSAIQNRFKYARVTPDTDWAHLLQDHPWLLSQSLVVKPDQLIKRRGKLGLVGVNLSLDG 80
Cdd:PLN02235 1 MARKKIREYDSKRLLKEHLKRLAGIDLPIRSAQVTESTDFNELANKEPWLSSTKLVVKPDMLFGKRGKSGLVALNLDLAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 81 VKSWLKPRLGHEATVGKAKGFLKNFLIEPFVPHSQaeEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKL 160
Cdd:PLN02235 81 VATFVKERLGKEVEMGGCKGPITTFIVEPFVPHDQ--EFYLSIVSDRLGCSISFSECGGIEIEENWDKVKTIFLPTEAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 161 nTEDIKRHLLVHAPEDKKEVLASFISGLFNFYEDLYFTYLEINPLVVTKDGVYILDLAAKVDATADYICKVKWGDIEFPP 240
Cdd:PLN02235 159 -TSEICAPLIATLPLEIRGKIEEFIKGVFAVFQDLDFTFLEMNPFTLVDGEPYPLDMRGELDDTAAFKNFKKWGNIEFPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 241 PFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYA 320
Cdd:PLN02235 238 PFGRVMSPTESFIHGLDEKTSASLKFTVLNPKGRIWTMVAGGGASVIYADTVGDLGYASELGNYAEYSGAPNEEEVLQYA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 321 KTILSLMTreKHPEGK--ILIIGGSIANFTNVAATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTT 398
Cdd:PLN02235 318 RVVIDCAT--ANPDGRkrALLIGGGIANFTDVAATFNGIIRALREKESKLKAARMHIFVRRGGPNYQKGLAKMRALGEEI 395
|
410 420
....*....|....*....|.
gi 313151222 399 GIPIHVFGTETHMTAIVGMAL 419
Cdd:PLN02235 396 GVPIEVYGPEATMTGICKQAI 416
|
|
| Citrate_bind |
pfam16114 |
ATP citrate lyase citrate-binding; This is the citrate-binding domain of ATP citrate lyase. ... |
244-421 |
1.01e-122 |
|
ATP citrate lyase citrate-binding; This is the citrate-binding domain of ATP citrate lyase. This domain has a Rossmann fold.
Pssm-ID: 465025 Cd Length: 178 Bit Score: 373.14 E-value: 1.01e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 244 REAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYAKTI 323
Cdd:pfam16114 1 RELSPEEAYIAELDAKTGASLKLTILNPKGRIWTMVAGGGASVVYADTIADLGGASELANYGEYSGAPSETQTYEYAKTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 324 LSLMTREKHPEGKILIIGGSIANFTNVAATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIH 403
Cdd:pfam16114 81 LDLMTREPHPDGKVLIIGGGIANFTDVAATFKGIIRALREYKSKLKEHKVKIWVRRGGPNYQEGLRAMRALGEELGLPIH 160
|
170
....*....|....*...
gi 313151222 404 VFGTETHMTAIVGMALGH 421
Cdd:pfam16114 161 VYGPETHMTGIVPMALGY 178
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
856-1093 |
5.95e-92 |
|
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. CCL cleaves citryl-CoA (CiCoA) to acetyl-CoA (AcCoA) and oxaloacetate (OAA). ACL catalyzes an ATP- and a CoA- dependant cleavage of citrate to form AcCoA and OAA in a multistep reaction, the final step of which is likely to involve the cleavage of CiCoA to generate AcCoA and OAA. In fungi, yeast, plants, and animals ACL is cytosolic and generates AcCoA for lipogenesis. ACL may be required for fruiting body maturation in the filamentous fungus Sordaria macrospore. 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; the first enzyme is citryl-CoA synthetase (CCS) which is not included in this group. Chlorobium limicola ACL is an example of a two-subunit type ACL. It is comprised of a large and a small subunit; it has been speculated that the large subunit arose from a fusion of the small subunit of the two subunit CCS with CCL. The small ACL subunit is a homolog of the larger CCS subunit. Mammalian ACL is of the single-subunit type and may have arisen from the two-subunit ACL by another gene fusion. Mammalian ACLs are homotetramers; the ACLs of C. limicola and Arabidopsis are a heterooctomers (alpha4beta4). In cancer cells there is a shift in energy metabolism to aerobic glycolysis, the glycolytic end product pyruvate enters a truncated TCA cycle generating citrate which is cleaved in the cytosol by ACL. Inhibiting ACL limits the in-vitro proliferation and survival of these cancer cells, reduces in vivo tumor growth, and induces differentiation.
Pssm-ID: 99854 [Multi-domain] Cd Length: 227 Bit Score: 293.32 E-value: 5.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 856 GMPITEVFKEeMGIGGVLGLLWFQRRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICARAG-KDLVSSLTSGLLTIGDR 934
Cdd:cd06100 1 GYDLSDLIGK-ISFGDVLYLLLKGRLPTPYEARLLEALLVALADHGPATPSAHAARLTASAGpEDLQSAVAAGLLGIGDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 935 FGGALDAAAKMFSKAFDSGI----IPMEFVNKMKKEGKLIMGIGHRVKSinNPDMRVQILKDFVKQHFPATPLLDYALEV 1010
Cdd:cd06100 80 FGGAGEGAARLFKEAVDSGDaldaAAAEFVAEYRAAKKRIPGFGHPVHK--NPDPRVPRLLELARELGPAGPHLDYALAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 1011 EKITTSKKP-NLILNVDGFIGVAFVDMlrncGSFTreeadeyvdiGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWD 1089
Cdd:cd06100 158 EKALTAAKGkPLPLNVDGAIAAILLDL----GFPP----------GALRGLFVLGRSPGLIAHALEEKRLGQPLYRHPWD 223
|
....
gi 313151222 1090 DISY 1093
Cdd:cd06100 224 DIEY 227
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
550-802 |
2.01e-51 |
|
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA synthetase, alpha subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439844 [Multi-domain] Cd Length: 288 Bit Score: 182.95 E-value: 2.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 550 IPVFKNMADAMKKHPevdvlINfASL-----RSAYDSTMETMNyAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPA 624
Cdd:COG0074 50 VPVFDTVAEAVEETG-----AD-ASVifvppPFAADAILEAID-AGIKLIVCITEGIPVLDMVRVKRYAKAKGTRLIGPN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 625 TVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRY 704
Cdd:COG0074 123 CPGIITPGECKLG--------IMPGHIFKPGRVGIVSRSGTLTYEAVWQLTQAGLGQSTCVGIGGDPIIGTSFIDVLELF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 705 QDTPGVKMIVVLGEIGGTEEYKICRGIKEGrLTKPVVCWCIGTCAtmfSSEVQFGHAGACANQASETAVAKNQALKEAGV 784
Cdd:COG0074 195 EEDPETEAIVMIGEIGGSAEEEAAEYIKEN-MTKPVVAYIAGRTA---PPGKRMGHAGAIISGGKGTAESKIEALEAAGV 270
|
250
....*....|....*...
gi 313151222 785 FVPRSFDELGEIIQSVYE 802
Cdd:COG0074 271 PVAESPSEIGELLKKALK 288
|
|
| sucCoAalpha |
TIGR01019 |
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha ... |
544-800 |
4.50e-38 |
|
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha subunits but does not discriminate between GTP-specific and ATP-specific reactions. The model is designated as subfamily rather than equivalog for that reason. ATP citrate lyases appear to form an outgroup. [Energy metabolism, TCA cycle]
Pssm-ID: 130091 [Multi-domain] Cd Length: 286 Bit Score: 144.10 E-value: 4.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 544 GHKEILIPVFKNMADAMKKhPEVDVLINFASLRSAYDSTMETMNyAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGP 623
Cdd:TIGR01019 43 GTTVLGLPVFDSVKEAVEE-TGANASVIFVPAPFAADAIFEAID-AGIELIVCITEGIPVHDMLKVKRYMEESGTRLIGP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 624 ATVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNElnnIISRTTD---GVYEGVAIGGDRYPGSTFMDH 700
Cdd:TIGR01019 121 NCPGIITPGECKIG--------IMPGHIHKPGNVGIVSRSGTLTYE---AVHQLTKagfGQSTCVGIGGDPVNGTSFIDV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 701 VLRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEgRLTKPVVCWCIGTCA----TMfssevqfGHAGACANQASETAVAKN 776
Cdd:TIGR01019 190 LEAFEKDPETEAIVMIGEIGGSAEEEAADFIKQ-NMSKPVVGFIAGATAppgkRM-------GHAGAIISGGKGTAESKI 261
|
250 260
....*....|....*....|....
gi 313151222 777 QALKEAGVFVPRSFDELGEIIQSV 800
Cdd:TIGR01019 262 EALEAAGVTVVKSPSDIGELLAEI 285
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
890-1078 |
5.80e-21 |
|
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: 96.04 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 890 IEMCLMVTADHGPAVSgAHNTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPmEFVNKMK-KEG 967
Cdd:pfam00285 170 LDLYLILHADHEGNAS-TFTARVVASTLADPYSAIAAAIGALkGPLHGGANEAVLEMLEEIGSPDEVE-EYIRKVLnKGK 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 968 KLIMGIGHRV-KsinNPDMRVQILKDFVKQHFPAT---PLLDYALEVEKIT----TSKKPNLILNVDGFIGVAF------ 1033
Cdd:pfam00285 248 ERIMGFGHRVyK---NYDPRAKILKEFAEELAEEGgddPLLELAEELEEVApedlYFVEKNLYPNVDFYSGVLYhalgip 324
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 313151222 1034 VDMlrncgsFTreeadeyvdigalnGIFVLGRSMGFIGHYLDQKR 1078
Cdd:pfam00285 325 TDM------FT--------------PLFAISRTAGWLAHWIEQLA 349
|
|
| sucCoAbeta |
TIGR01016 |
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ... |
54-403 |
3.90e-14 |
|
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not discriminate the ADP-forming enzyme ((EC 6.2.1.5) from the GDP_forming (EC 6.2.1.4) enzyme. The N-terminal half is described by the CoA-ligases model (pfam00549). The C-terminal half is described by the ATP-grasp model (pfam02222). This family contains a split seen both in a maximum parsimony tree (which ignores gaps) and in the gap pattern near position 85 of the seed alignment. Eukaryotic and most bacterial sequences are longer and contain a region similar to TXQTXXXG. Sequences from Deinococcus radiodurans, Mycobacterium tuberculosis, Streptomyces coelicolor, and the Archaea are 6 amino acids shorter in that region and contain a motif resembling [KR]G [Energy metabolism, TCA cycle]
Pssm-ID: 273396 [Multi-domain] Cd Length: 386 Bit Score: 75.49 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 54 SLVVKPDQLIKRRGKLGLVGVNLSLDGVKSWLKPRLGHE-ATVGKAKGFLK--NFLIEPFVPhsQAEEFYVCIYATREGD 130
Cdd:TIGR01016 42 PVVVKAQVHAGGRGKAGGVKVAKSKEEARAAAEKLLGKElVTNQTDPLGQPvnKILIEEATD--IDKEYYLSIVIDRSAR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 131 YVLF--HHEGGVDVGDVDAKAQKLL--VGVDEKLNTED-IKRHLLVHAPEDKKEV--LASFISGLFNFYEDLYFTYLEIN 203
Cdd:TIGR01016 120 CPVImaSTEGGVDIEEVAEKSPEKIikYAIDPLTGLLPyQAREIAKKLGLEGELVkqVADIIKKLYQIFLEYDASLVEIN 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 204 PLVVTKDG-VYILDLAAKVDATADYickvKWGDIEfpppfgrEAY-PEEAYIADLDAKsgaSLKLTLLNPKGRIWTMVAG 281
Cdd:TIGR01016 200 PLVITKDGnLIALDAKLTIDDNALF----RHPDLE-------EMRdYSQEDPREVLAK---QWGLNYVALDGNIGCMVNG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 282 GGASVVYSDTICDLGGvnELANYGEYSGAPSEQQTYDYAKTILSlmtrekHPEGKILIIG--GSIANFTNVAatfKGIVR 359
Cdd:TIGR01016 266 AGLAMATMDIIKLYGG--EPANFLDVGGGASAERVREALKLVLS------DKSVKVVFINifGGITRCDLVA---KGLVE 334
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 313151222 360 AIRDyqgplKEHEVTIFVRRGGPNYQEGLRVMGEvgktTGIPIH 403
Cdd:TIGR01016 335 ALKE-----VGVNVPVVVRLEGTNVEEGKKILAE----SGLNII 369
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
492-601 |
1.54e-08 |
|
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.
Pssm-ID: 214881 [Multi-domain] Cd Length: 100 Bit Score: 53.28 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 492 LFSRHTKAIVWGMQTRAVQgMLDFDYVCSRDEPSVaaMVYPFTGDHKQKFYWGhkeilIPVFKNMADAMKKHpEVDVLIN 571
Cdd:smart00881 1 LLNPNTSVAVVGASGNLGS-FGLAVMRNLLEYGTK--FVGGVYPGKVGPKVDG-----VPVYDSVAEAPEET-GVDVAVI 71
|
90 100 110
....*....|....*....|....*....|
gi 313151222 572 FASLRSAYDSTMETMNyAQIRTIAIIAEGI 601
Cdd:smart00881 72 FVPAEAAPDAIDEAIE-AGIKGIVVITEGI 100
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
181-407 |
2.93e-06 |
|
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439815 [Multi-domain] Cd Length: 388 Bit Score: 50.82 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 181 LASFISGLFNFYEDLYFTYLEINPLVVTKDG-VYILDlaAKV--DATADY----IckVKWGDIEFPPPFGREAYPEE-AY 252
Cdd:COG0045 177 FAKILKKLYRAFVEKDASLVEINPLVVTKDGrLVALD--AKVnfDDNALFrhpeL--AALRDLSEEDPLEVEASKYGlNY 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 253 IAdLDaksgaslkltllnpkGRIWTMVAGGG---ASVvysDTICDLGGvnELANYGEYSGAPSEQQTYDYAKTILSlmtr 329
Cdd:COG0045 253 VK-LD---------------GNIGCMVNGAGlamATM---DIIKLAGG--EPANFLDVGGGATAERVAEAFKIILS---- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 330 ekHPEGK-ILI-IGGSIANFTNVAatfKGIVRAirdyqgpLKEHEVT--IFVRRGGPNYQEGLRVMGEvgktTGIPIHVF 405
Cdd:COG0045 308 --DPNVKaILVnIFGGITRCDVVA---EGIVAA-------LKEVGLKvpVVVRLEGTNVEEGRKILAE----SGLNIIAA 371
|
..
gi 313151222 406 GT 407
Cdd:COG0045 372 DT 373
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
489-1094 |
0e+00 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 952.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 489 SATLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPfTGDHKQKFYWGHKEILIPVFKNMADAMKKHPEVDV 568
Cdd:PLN02522 3 TGQLFSRTTQALFYNYKQLPVQRMLDFDFLCGRETPSVAGIINP-GSEGFQKLFFGQEEIAIPVHGSIEAACKAHPTADV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 569 LINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILA 648
Cdd:PLN02522 82 FINFASFRSAAASSMEALKQPTIRVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTLDNIIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 649 SKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIGGTEEYKIC 728
Cdd:PLN02522 162 CKLYRPGSVGFVSKSGGMSNEMYNVIARVTDGIYEGIAIGGDVFPGSTLSDHVLRFNNIPQIKMIVVLGELGGRDEYSLV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 729 RGIKEGRLTKPVVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVAKG 808
Cdd:PLN02522 242 EALKQGKVSKPVVAWVSGTCARLFKSEVQFGHAGAKSGGDMESAQAKNKALKDAGAIVPTSFEALEAAIKETFEKLVEEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 809 AIVPAQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQRRLPKYSCQ 888
Cdd:PLN02522 322 KIIPVKEVTPPQIPEDLNSAIKSGKVRAPTHIVSTISDDRGEEPCYAGVPMSSIIEKDYGVGDVISLLWFKRSLPRYCTK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 889 FIEMCLMVTADHGPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGK 968
Cdd:PLN02522 402 FIEMCIMLCADHGPCVSGAHNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDAYDRGLTPYEFVEGMKKKGI 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 969 LIMGIGHRVKSINNPDMRVQILKDFVKQHFPATPLLDYALEVEKITTSKKPNLILNVDGFIGVAFVDMLRNCGSFTREEA 1048
Cdd:PLN02522 482 RVPGIGHRIKSRDNRDKRVELLQKYARTHFPSVKYMEYAVQVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQEI 561
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 313151222 1049 DEYVDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYV 1094
Cdd:PLN02522 562 DEIVEIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYT 607
|
|
| PLN02235 |
PLN02235 |
ATP citrate (pro-S)-lyase |
1-419 |
8.70e-134 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 177879 [Multi-domain] Cd Length: 423 Bit Score: 412.24 E-value: 8.70e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 1 MSAKAISEQTGKELLYKYICTTSAIQNRFKYARVTPDTDWAHLLQDHPWLLSQSLVVKPDQLIKRRGKLGLVGVNLSLDG 80
Cdd:PLN02235 1 MARKKIREYDSKRLLKEHLKRLAGIDLPIRSAQVTESTDFNELANKEPWLSSTKLVVKPDMLFGKRGKSGLVALNLDLAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 81 VKSWLKPRLGHEATVGKAKGFLKNFLIEPFVPHSQaeEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKL 160
Cdd:PLN02235 81 VATFVKERLGKEVEMGGCKGPITTFIVEPFVPHDQ--EFYLSIVSDRLGCSISFSECGGIEIEENWDKVKTIFLPTEAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 161 nTEDIKRHLLVHAPEDKKEVLASFISGLFNFYEDLYFTYLEINPLVVTKDGVYILDLAAKVDATADYICKVKWGDIEFPP 240
Cdd:PLN02235 159 -TSEICAPLIATLPLEIRGKIEEFIKGVFAVFQDLDFTFLEMNPFTLVDGEPYPLDMRGELDDTAAFKNFKKWGNIEFPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 241 PFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYA 320
Cdd:PLN02235 238 PFGRVMSPTESFIHGLDEKTSASLKFTVLNPKGRIWTMVAGGGASVIYADTVGDLGYASELGNYAEYSGAPNEEEVLQYA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 321 KTILSLMTreKHPEGK--ILIIGGSIANFTNVAATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTT 398
Cdd:PLN02235 318 RVVIDCAT--ANPDGRkrALLIGGGIANFTDVAATFNGIIRALREKESKLKAARMHIFVRRGGPNYQKGLAKMRALGEEI 395
|
410 420
....*....|....*....|.
gi 313151222 399 GIPIHVFGTETHMTAIVGMAL 419
Cdd:PLN02235 396 GVPIEVYGPEATMTGICKQAI 416
|
|
| Citrate_bind |
pfam16114 |
ATP citrate lyase citrate-binding; This is the citrate-binding domain of ATP citrate lyase. ... |
244-421 |
1.01e-122 |
|
ATP citrate lyase citrate-binding; This is the citrate-binding domain of ATP citrate lyase. This domain has a Rossmann fold.
Pssm-ID: 465025 Cd Length: 178 Bit Score: 373.14 E-value: 1.01e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 244 REAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYAKTI 323
Cdd:pfam16114 1 RELSPEEAYIAELDAKTGASLKLTILNPKGRIWTMVAGGGASVVYADTIADLGGASELANYGEYSGAPSETQTYEYAKTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 324 LSLMTREKHPEGKILIIGGSIANFTNVAATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIH 403
Cdd:pfam16114 81 LDLMTREPHPDGKVLIIGGGIANFTDVAATFKGIIRALREYKSKLKEHKVKIWVRRGGPNYQEGLRAMRALGEELGLPIH 160
|
170
....*....|....*...
gi 313151222 404 VFGTETHMTAIVGMALGH 421
Cdd:pfam16114 161 VYGPETHMTGIVPMALGY 178
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
856-1093 |
5.95e-92 |
|
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. CCL cleaves citryl-CoA (CiCoA) to acetyl-CoA (AcCoA) and oxaloacetate (OAA). ACL catalyzes an ATP- and a CoA- dependant cleavage of citrate to form AcCoA and OAA in a multistep reaction, the final step of which is likely to involve the cleavage of CiCoA to generate AcCoA and OAA. In fungi, yeast, plants, and animals ACL is cytosolic and generates AcCoA for lipogenesis. ACL may be required for fruiting body maturation in the filamentous fungus Sordaria macrospore. 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; the first enzyme is citryl-CoA synthetase (CCS) which is not included in this group. Chlorobium limicola ACL is an example of a two-subunit type ACL. It is comprised of a large and a small subunit; it has been speculated that the large subunit arose from a fusion of the small subunit of the two subunit CCS with CCL. The small ACL subunit is a homolog of the larger CCS subunit. Mammalian ACL is of the single-subunit type and may have arisen from the two-subunit ACL by another gene fusion. Mammalian ACLs are homotetramers; the ACLs of C. limicola and Arabidopsis are a heterooctomers (alpha4beta4). In cancer cells there is a shift in energy metabolism to aerobic glycolysis, the glycolytic end product pyruvate enters a truncated TCA cycle generating citrate which is cleaved in the cytosol by ACL. Inhibiting ACL limits the in-vitro proliferation and survival of these cancer cells, reduces in vivo tumor growth, and induces differentiation.
Pssm-ID: 99854 [Multi-domain] Cd Length: 227 Bit Score: 293.32 E-value: 5.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 856 GMPITEVFKEeMGIGGVLGLLWFQRRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICARAG-KDLVSSLTSGLLTIGDR 934
Cdd:cd06100 1 GYDLSDLIGK-ISFGDVLYLLLKGRLPTPYEARLLEALLVALADHGPATPSAHAARLTASAGpEDLQSAVAAGLLGIGDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 935 FGGALDAAAKMFSKAFDSGI----IPMEFVNKMKKEGKLIMGIGHRVKSinNPDMRVQILKDFVKQHFPATPLLDYALEV 1010
Cdd:cd06100 80 FGGAGEGAARLFKEAVDSGDaldaAAAEFVAEYRAAKKRIPGFGHPVHK--NPDPRVPRLLELARELGPAGPHLDYALAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 1011 EKITTSKKP-NLILNVDGFIGVAFVDMlrncGSFTreeadeyvdiGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWD 1089
Cdd:cd06100 158 EKALTAAKGkPLPLNVDGAIAAILLDL----GFPP----------GALRGLFVLGRSPGLIAHALEEKRLGQPLYRHPWD 223
|
....
gi 313151222 1090 DISY 1093
Cdd:cd06100 224 DIEY 227
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
550-802 |
2.01e-51 |
|
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA synthetase, alpha subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439844 [Multi-domain] Cd Length: 288 Bit Score: 182.95 E-value: 2.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 550 IPVFKNMADAMKKHPevdvlINfASL-----RSAYDSTMETMNyAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPA 624
Cdd:COG0074 50 VPVFDTVAEAVEETG-----AD-ASVifvppPFAADAILEAID-AGIKLIVCITEGIPVLDMVRVKRYAKAKGTRLIGPN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 625 TVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRY 704
Cdd:COG0074 123 CPGIITPGECKLG--------IMPGHIFKPGRVGIVSRSGTLTYEAVWQLTQAGLGQSTCVGIGGDPIIGTSFIDVLELF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 705 QDTPGVKMIVVLGEIGGTEEYKICRGIKEGrLTKPVVCWCIGTCAtmfSSEVQFGHAGACANQASETAVAKNQALKEAGV 784
Cdd:COG0074 195 EEDPETEAIVMIGEIGGSAEEEAAEYIKEN-MTKPVVAYIAGRTA---PPGKRMGHAGAIISGGKGTAESKIEALEAAGV 270
|
250
....*....|....*...
gi 313151222 785 FVPRSFDELGEIIQSVYE 802
Cdd:COG0074 271 PVAESPSEIGELLKKALK 288
|
|
| sucCoAalpha |
TIGR01019 |
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha ... |
544-800 |
4.50e-38 |
|
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha subunits but does not discriminate between GTP-specific and ATP-specific reactions. The model is designated as subfamily rather than equivalog for that reason. ATP citrate lyases appear to form an outgroup. [Energy metabolism, TCA cycle]
Pssm-ID: 130091 [Multi-domain] Cd Length: 286 Bit Score: 144.10 E-value: 4.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 544 GHKEILIPVFKNMADAMKKhPEVDVLINFASLRSAYDSTMETMNyAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGP 623
Cdd:TIGR01019 43 GTTVLGLPVFDSVKEAVEE-TGANASVIFVPAPFAADAIFEAID-AGIELIVCITEGIPVHDMLKVKRYMEESGTRLIGP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 624 ATVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNElnnIISRTTD---GVYEGVAIGGDRYPGSTFMDH 700
Cdd:TIGR01019 121 NCPGIITPGECKIG--------IMPGHIHKPGNVGIVSRSGTLTYE---AVHQLTKagfGQSTCVGIGGDPVNGTSFIDV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 701 VLRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEgRLTKPVVCWCIGTCA----TMfssevqfGHAGACANQASETAVAKN 776
Cdd:TIGR01019 190 LEAFEKDPETEAIVMIGEIGGSAEEEAADFIKQ-NMSKPVVGFIAGATAppgkRM-------GHAGAIISGGKGTAESKI 261
|
250 260
....*....|....*....|....
gi 313151222 777 QALKEAGVFVPRSFDELGEIIQSV 800
Cdd:TIGR01019 262 EALEAAGVTVVKSPSDIGELLAEI 285
|
|
| PRK05678 |
PRK05678 |
succinyl-CoA synthetase subunit alpha; Validated |
550-804 |
1.07e-37 |
|
succinyl-CoA synthetase subunit alpha; Validated
Pssm-ID: 180194 [Multi-domain] Cd Length: 291 Bit Score: 143.39 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 550 IPVFKNMADAMKKHpEVDVLINFASLRSAYDSTMETMNyAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPATVGGI 629
Cdd:PRK05678 51 LPVFNTVAEAVEAT-GANASVIYVPPPFAADAILEAID-AGIDLIVCITEGIPVLDMLEVKAYLERKKTRLIGPNCPGII 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 630 KPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNElnnIISRTTD---GVYEGVAIGGDRYPGSTFMDHVLRYQD 706
Cdd:PRK05678 129 TPGECKIG--------IMPGHIHKKGRVGVVSRSGTLTYE---AVAQLTDlgfGQSTCVGIGGDPINGTNFIDVLEAFEE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 707 TPGVKMIVVLGEIGGTEEYKICRGIKEgRLTKPVVCWCIGTCA----TMfssevqfGHAGACANQASETAVAKNQALKEA 782
Cdd:PRK05678 198 DPETEAIVMIGEIGGSAEEEAAEYIKA-NVTKPVVGYIAGVTAppgkRM-------GHAGAIISGGKGTAEEKKEALEAA 269
|
250 260
....*....|....*....|..
gi 313151222 783 GVFVPRSFDELGEIIQSVYEDL 804
Cdd:PRK05678 270 GVKVARTPSEIGELLKEVLKGL 291
|
|
| PTZ00187 |
PTZ00187 |
succinyl-CoA synthetase alpha subunit; Provisional |
545-805 |
5.08e-34 |
|
succinyl-CoA synthetase alpha subunit; Provisional
Pssm-ID: 240307 [Multi-domain] Cd Length: 317 Bit Score: 133.30 E-value: 5.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 545 HKEILIPVFKNMADAmKKHPEVDVLINFASLRSAYDSTMETMNyAQIRTIAIIAEGIPEALTRKlIKKA--DQKGVTIIG 622
Cdd:PTZ00187 69 HLKHGLPVFATVKEA-KKATGADASVIYVPPPHAASAIIEAIE-AEIPLVVCITEGIPQHDMVK-VKHAllSQNKTRLIG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 623 PATVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVL 702
Cdd:PTZ00187 146 PNCPGIIKPGECKIG--------IMPGHIHKKGKIGIVSRSGTLTYEAVAQTTAVGLGQSTCVGIGGDPFNGTNFIDCLK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 703 RYQDTPGVKMIVVLGEIGGTEEYKICRGIKEGRLTKPVVCWCIGTCAtmfSSEVQFGHAGACANQASETAVAKNQALKEA 782
Cdd:PTZ00187 218 LFLNDPETEGIILIGEIGGTAEEEAAEWIKNNPIKKPVVSFIAGITA---PPGRRMGHAGAIISGGKGTAPGKIEALEAA 294
|
250 260
....*....|....*....|...
gi 313151222 783 GVFVPRSFDELGEIIQSVYEDLV 805
Cdd:PTZ00187 295 GVRVVKSPAQLGKTMLEVMKKKG 317
|
|
| PLN00125 |
PLN00125 |
Succinyl-CoA ligase [GDP-forming] subunit alpha |
544-803 |
2.69e-28 |
|
Succinyl-CoA ligase [GDP-forming] subunit alpha
Pssm-ID: 215066 [Multi-domain] Cd Length: 300 Bit Score: 116.22 E-value: 2.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 544 GHKEILIPVFKNMADAmKKHPEVDVLINFASLRSAYDSTMETMNyAQIRTIAIIAEGIPEALTRKlIKKA--DQKGVTII 621
Cdd:PLN00125 49 GTEHLGLPVFNTVAEA-KAETKANASVIYVPPPFAAAAILEAME-AELDLVVCITEGIPQHDMVR-VKAAlnRQSKTRLI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 622 GPATVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHV 701
Cdd:PLN00125 126 GPNCPGIIKPGECKIG--------IMPGYIHKPGRIGIVSRSGTLTYEAVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 702 LRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEGRLTKPVVCWCIGTCAtmfSSEVQFGHAGACANQASETAVAKNQALKE 781
Cdd:PLN00125 198 EKFVKDPQTEGIILIGEIGGTAEEDAAAFIKESGTEKPVVAFIAGLTA---PPGRRMGHAGAIVSGGKGTAQDKIKALRE 274
|
250 260
....*....|....*....|..
gi 313151222 782 AGVFVPRSFDELGEIIQSVYED 803
Cdd:PLN00125 275 AGVTVVESPAKIGVAMLEVFKE 296
|
|
| CS_ACL-C_CCL |
cd06099 |
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ... |
890-1085 |
4.09e-22 |
|
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: 95.87 E-value: 4.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 890 IEMCLMVTADHGPAVSgAHNTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPMEF-VNKMKKEG 967
Cdd:cd06099 23 MDLALILHADHEGNAS-TFTARVVGSTGSDPYSAIAAAIGALkGPLHGGANEAVLKMLEEIGTPKNEPAEAyIRKKLESK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 968 KLIMGIGHRVKSinNPDMRVQILKDFVKQHFPAT---PLLDYALEVEKITTSKKP--NLILNVDGFIGVAFVDMlrncGs 1042
Cdd:cd06099 102 RVIMGFGHRVYK--KYDPRATVLKKFAEELLKEDgddPMFELAAELEKIAEEVLYekKLYPNVDFYSGVLYKAM----G- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 313151222 1043 ftreeadeyVDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYR 1085
Cdd:cd06099 175 ---------FPTELFTPLFAVARAVGWLAHLIEQLEDNFKIIR 208
|
|
| citrate_synt |
cd06101 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
842-1085 |
9.35e-22 |
|
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: 96.23 E-value: 9.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 842 TSICDERGQE--LIYAGMPITEVfKEEMGIGGVLGLLWFqRRLPKYSCQFIEM----------------CLMVTADHGPA 903
Cdd:cd06101 11 SEISVIDGDEggLRYRGYPIEEL-AENSSFEEVAYLLLT-GELPSYAENFLYMlggeepdpefakamdlALILHADHEGN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 904 VSgAHNTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPMEF-VNKMKKEGKLIMGIGHRVKSin 981
Cdd:cd06101 89 AS-TFTARVVGSTLSDPYSAIAAAIAALkGPLHGGANEAVLKMLEEIGTPKNEPAEAyIRKKLNSKRVLMGFGHRVYK-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 982 NPDMRVQILKDFVKQHFPAT---PLLDYALEVEKITTSKKP--NLILNVDGFIGVAFVDMlrncGsftreeadeyVDIGA 1056
Cdd:cd06101 166 KYDPRATVLKKFAEKLLKEKgldPMFELAAELEKIAPEVLYekKLYPNVDFYSGVLYKAM----G----------FPTEL 231
|
250 260
....*....|....*....|....*....
gi 313151222 1057 LNGIFVLGRSMGFIGHYLDQKRLKQGLYR 1085
Cdd:cd06101 232 FTPLFAVSRAVGWLAHLIEQREDGQRIIR 260
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
842-1097 |
3.10e-21 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 94.55 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 842 TSICDERGQELIYAGMPITEVFkEEMGIGGVLGLLWFQRRLPKYSCQFIEMCLMVTADHGPAVSgahntIICAR----AG 917
Cdd:PRK06224 11 TSISDVTPEEIYVRGYDLEDLI-GKLSFTDMIFLLLRGRLPTPNEARLLDAVLVALVDHGLTPS-----AAAARmtasGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 918 KDLVSSLTSGLLTIGDRFGGALDAAAKMFS---KAFDSGIIPME----FVNKMKKEGKLIMGIGHRVKSINNPdmRVQIL 990
Cdd:PRK06224 85 ESLQGAVAAGLLALGSVHGGAGEQAAELLQeiaAAADAGADLDAaaraIVAEYRAAGKRVPGFGHPLHKPVDP--RAPRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 991 KDFVKQHFPATPLLDYALEVEKI--TTSKKPnLILNVDGFIGVAFVDMlrncGsftreeadeyVDIGALNGIFVLGRSMG 1068
Cdd:PRK06224 163 LALAREAGVAGRHCRLAEALEAAlaAAKGKP-LPLNVDGAIAAILADL----G----------FPPALARGLFVISRAAG 227
|
250 260 270
....*....|....*....|....*....|.
gi 313151222 1069 FIGHYLDQKRLKQG--LYRHPWDDISYVLPE 1097
Cdd:PRK06224 228 LVAHVWEELQQPIGfrIWDPAEEAVEYTGPP 258
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
890-1078 |
5.80e-21 |
|
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: 96.04 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 890 IEMCLMVTADHGPAVSgAHNTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPmEFVNKMK-KEG 967
Cdd:pfam00285 170 LDLYLILHADHEGNAS-TFTARVVASTLADPYSAIAAAIGALkGPLHGGANEAVLEMLEEIGSPDEVE-EYIRKVLnKGK 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 968 KLIMGIGHRV-KsinNPDMRVQILKDFVKQHFPAT---PLLDYALEVEKIT----TSKKPNLILNVDGFIGVAF------ 1033
Cdd:pfam00285 248 ERIMGFGHRVyK---NYDPRAKILKEFAEELAEEGgddPLLELAEELEEVApedlYFVEKNLYPNVDFYSGVLYhalgip 324
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 313151222 1034 VDMlrncgsFTreeadeyvdigalnGIFVLGRSMGFIGHYLDQKR 1078
Cdd:pfam00285 325 TDM------FT--------------PLFAISRTAGWLAHWIEQLA 349
|
|
| Ligase_CoA |
pfam00549 |
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ... |
660-785 |
8.33e-21 |
|
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, malate CoA ligase and ATP-citrate lyase. Some members of the family utilize ATP others use GTP.
Pssm-ID: 395434 [Multi-domain] Cd Length: 128 Bit Score: 89.24 E-value: 8.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 660 VSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIG-GTEEYK---ICRGIKEGR 735
Cdd:pfam00549 1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAFTPTTRIDALKLEAADPEVKVILLDIVLGyGACEDPaggLLKAIKEAR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 313151222 736 -LTKPVVCWCIGTCAtmfSSEVQFGHAGACANQASETAVAKNQALKEAGVF 785
Cdd:pfam00549 81 aRELPVVARVCGTEA---DPQGRSGQAKALAESGVLIASSNNQALRAAGAV 128
|
|
| GltA |
COG0372 |
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ... |
891-1085 |
6.21e-17 |
|
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: 83.99 E-value: 6.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 891 EMCLMVTADHGPAVSgAHNTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPmEFVNKMKKEGKL 969
Cdd:COG0372 185 DLLLILHADHEQNAS-TFTARVVASTLADLYSAIAAAIGALkGPLHGGANEAVLEMLEEIGSPDNVE-EYIRKALDKKER 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 970 IMGIGHRV-KsinNPDMRVQILKDFVKQHFPAT---PLLDYALEVEKITTSKKP----NLILNVDGFIGVAF------VD 1035
Cdd:COG0372 263 IMGFGHRVyK---NYDPRAKILKEAAEELLEELgddPLLEIAEELEEVALEDEYfiekKLYPNVDFYSGIVYhalgipTD 339
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 313151222 1036 MlrncgsFTreeadeyvdigalnGIFVLGRSMGFIGHYLDQkRLKQGLYR 1085
Cdd:COG0372 340 M------FT--------------PIFAISRVAGWIAHWLEQ-RADNRIIR 368
|
|
| citrate_synt_like_1 |
cd06118 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
890-1085 |
7.54e-16 |
|
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: 80.34 E-value: 7.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 890 IEMCLMVTADHGPAVSgAHNTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMF------SKAFdsgiipmEFVNK 962
Cdd:cd06118 170 MDLALILHADHEGNAS-TFTARVVASTLSDMYSAIAAAIAALkGPLHGGANEAVLKMLleigtpENVE-------AYIWK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 963 MKKEGKLIMGIGHRVKSinNPDMRVQILKDFVKQHFP---ATPLLDYALEVEKITTSKKP--NLILNVDGFIGVAFVDMl 1037
Cdd:cd06118 242 KLANKRRIMGFGHRVYK--TYDPRAKILKELAEELAEekgDDKLFEIAEELEEIALEVLGekGIYPNVDFYSGVVYKAL- 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 313151222 1038 rncGsftreeadeyVDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYR 1085
Cdd:cd06118 319 ---G----------FPTELFTPLFAVSRAVGWLAHIIEYRENNQRLIR 353
|
|
| sucCoAbeta |
TIGR01016 |
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ... |
54-403 |
3.90e-14 |
|
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not discriminate the ADP-forming enzyme ((EC 6.2.1.5) from the GDP_forming (EC 6.2.1.4) enzyme. The N-terminal half is described by the CoA-ligases model (pfam00549). The C-terminal half is described by the ATP-grasp model (pfam02222). This family contains a split seen both in a maximum parsimony tree (which ignores gaps) and in the gap pattern near position 85 of the seed alignment. Eukaryotic and most bacterial sequences are longer and contain a region similar to TXQTXXXG. Sequences from Deinococcus radiodurans, Mycobacterium tuberculosis, Streptomyces coelicolor, and the Archaea are 6 amino acids shorter in that region and contain a motif resembling [KR]G [Energy metabolism, TCA cycle]
Pssm-ID: 273396 [Multi-domain] Cd Length: 386 Bit Score: 75.49 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 54 SLVVKPDQLIKRRGKLGLVGVNLSLDGVKSWLKPRLGHE-ATVGKAKGFLK--NFLIEPFVPhsQAEEFYVCIYATREGD 130
Cdd:TIGR01016 42 PVVVKAQVHAGGRGKAGGVKVAKSKEEARAAAEKLLGKElVTNQTDPLGQPvnKILIEEATD--IDKEYYLSIVIDRSAR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 131 YVLF--HHEGGVDVGDVDAKAQKLL--VGVDEKLNTED-IKRHLLVHAPEDKKEV--LASFISGLFNFYEDLYFTYLEIN 203
Cdd:TIGR01016 120 CPVImaSTEGGVDIEEVAEKSPEKIikYAIDPLTGLLPyQAREIAKKLGLEGELVkqVADIIKKLYQIFLEYDASLVEIN 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 204 PLVVTKDG-VYILDLAAKVDATADYickvKWGDIEfpppfgrEAY-PEEAYIADLDAKsgaSLKLTLLNPKGRIWTMVAG 281
Cdd:TIGR01016 200 PLVITKDGnLIALDAKLTIDDNALF----RHPDLE-------EMRdYSQEDPREVLAK---QWGLNYVALDGNIGCMVNG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 282 GGASVVYSDTICDLGGvnELANYGEYSGAPSEQQTYDYAKTILSlmtrekHPEGKILIIG--GSIANFTNVAatfKGIVR 359
Cdd:TIGR01016 266 AGLAMATMDIIKLYGG--EPANFLDVGGGASAERVREALKLVLS------DKSVKVVFINifGGITRCDLVA---KGLVE 334
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 313151222 360 AIRDyqgplKEHEVTIFVRRGGPNYQEGLRVMGEvgktTGIPIH 403
Cdd:TIGR01016 335 ALKE-----VGVNVPVVVRLEGTNVEEGKKILAE----SGLNII 369
|
|
| PLN02456 |
PLN02456 |
citrate synthase |
891-1073 |
2.39e-11 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 67.36 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 891 EMCLMVTADHGPAVSGAHNTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPmEFVNKMKKEGKL 969
Cdd:PLN02456 249 DLYFIIHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALaGPLHGGANEAVLKMLKEIGTVENIP-EYVEGVKNSKKV 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 970 IMGIGHRVksINNPDMRVQILKDF---VKQHFPATPLLDYALEVEKITTS----KKPNLILNVDGFIGVafvdMLRNCGs 1042
Cdd:PLN02456 328 LPGFGHRV--YKNYDPRAKCIREFaleVFKHVGDDPLFKVASALEEVALLdeyfKVRKLYPNVDFYSGV----LLRALG- 400
|
170 180 190
....*....|....*....|....*....|.
gi 313151222 1043 FTReeadEYVDIgalngIFVLGRSMGFIGHY 1073
Cdd:PLN02456 401 FPE----EFFTV-----LFAVSRAAGYLSQW 422
|
|
| cit_synth_II |
TIGR01800 |
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ... |
891-1076 |
7.60e-11 |
|
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with activity as 2-methylcitrate synthase, citrate synthase, or both. Many Gram-negative species have a hexameric citrate synthase, termed citrate synthase I (TIGR01798). Members of this family (TIGR01800) appear as a second citrate synthase isozyme but typically are associated with propionate metabolism and synthesize 2-methylcitrate from propionyl-CoA; citrate synthase activity may be incidental. A number of species, including Thermoplasma acidophilum, Pyrococcus furiosus, and the Antarctic bacterium DS2-3R have a bifunctional member of this family as the only citrate synthase isozyme.
Pssm-ID: 130859 Cd Length: 368 Bit Score: 65.08 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 891 EMCLMVTADHG-PAVSGAhnTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFsKAFDSGIIPMEFVNKMKKEGK 968
Cdd:TIGR01800 171 DIALILYAEHEfNASTFA--ARVIASTLSDMYSAITAAIGALkGPLHGGANEAVMAML-DEIGDPDKAEAWIRKALENKE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 969 LIMGIGHRVKSINNPdmRVQILKDFVKQHFPATPLLDY---ALEVEKITTSKKpNLILNVDGFIGVAFVDMlrncGsftr 1045
Cdd:TIGR01800 248 RIMGFGHRVYKTYDP--RAKILKEYAKKLSAKEGSSKWyeiAERLEDVMEEEK-GIYPNVDFFSASVYYMM----G---- 316
|
170 180 190
....*....|....*....|....*....|.
gi 313151222 1046 eeadeyVDIGALNGIFVLGRSMGFIGHYLDQ 1076
Cdd:TIGR01800 317 ------IPTDLFTPIFAMSRVTGWTAHIIEQ 341
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
492-601 |
1.54e-08 |
|
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.
Pssm-ID: 214881 [Multi-domain] Cd Length: 100 Bit Score: 53.28 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 492 LFSRHTKAIVWGMQTRAVQgMLDFDYVCSRDEPSVaaMVYPFTGDHKQKFYWGhkeilIPVFKNMADAMKKHpEVDVLIN 571
Cdd:smart00881 1 LLNPNTSVAVVGASGNLGS-FGLAVMRNLLEYGTK--FVGGVYPGKVGPKVDG-----VPVYDSVAEAPEET-GVDVAVI 71
|
90 100 110
....*....|....*....|....*....|
gi 313151222 572 FASLRSAYDSTMETMNyAQIRTIAIIAEGI 601
Cdd:smart00881 72 FVPAEAAPDAIDEAIE-AGIKGIVVITEGI 100
|
|
| CoA_binding |
pfam02629 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
497-600 |
7.61e-08 |
|
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.
Pssm-ID: 396961 [Multi-domain] Cd Length: 97 Bit Score: 51.05 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 497 TKAIVWGMQTRAVQGM-LDFDYVCSRDEPSVAAMVYPFTGDhkqkfywghkEIL-IPVFKNMADAMKKHpEVDVLINFAS 574
Cdd:pfam02629 4 TKVIVIGAGGLGIQGLnYHFIQMLGYGIKMVFGVNPGKGGT----------EILgIPVYNSVDELEEKT-GVDVAVITVP 72
|
90 100
....*....|....*....|....*.
gi 313151222 575 LRSAYDSTMETMNyAQIRTIAIIAEG 600
Cdd:pfam02629 73 APFAQEAIDELVD-AGIKGIVNITPG 97
|
|
| gltA |
PRK05614 |
citrate synthase; |
936-1076 |
3.59e-07 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 53.73 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 936 GGALDAAAKMFSKAFDSGIIPmEFVNKMK-KEG--KLiMGIGHRVksINNPDMRVQILK---DFVKQHFPA-TPLLDYAL 1008
Cdd:PRK05614 268 GGANEAVLKMLEEIGSVDNIP-EFIARAKdKNDgfRL-MGFGHRV--YKNYDPRAKIMRetcHEVLKELGLnDPLLEVAM 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 1009 EVEKITT------SKKpnLILNVDGFIGVAF------VDMlrncgsFTreeadeyvdigalnGIFVLGRSMGFIGHYLDQ 1076
Cdd:PRK05614 344 ELEEIALndeyfiERK--LYPNVDFYSGIILkalgipTSM------FT--------------VIFALARTVGWIAHWNEM 401
|
|
| BsCS-I_like |
cd06109 |
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ... |
890-1078 |
5.29e-07 |
|
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: 53.08 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 890 IEMCLMVTADHGPAVSGAHNTIIcARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKeGK 968
Cdd:cd06109 159 LDAYLVTVADHGMNASTFTARVI-ASTEADLTSAVLGAIGALkGPLHGGAPGPVLDMLDAIGTPENAEAWLREALAR-GE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 969 LIMGIGHRVKSINNPdmRVQILKDFVKQHFPATPLLDYALEVEKITTS----KKPN--LILNVDGFIGVafvdMLRNCGs 1042
Cdd:cd06109 237 RLMGFGHRVYRVRDP--RADVLKAAAERLGAPDERLEFAEAVEQAALAllreYKPGrpLETNVEFYTAL----LLEALG- 309
|
170 180 190
....*....|....*....|....*....|....*.
gi 313151222 1043 FTREeadeyvdigALNGIFVLGRSMGFIGHYLDQKR 1078
Cdd:cd06109 310 LPRE---------AFTPTFAAGRTAGWTAHVLEQAR 336
|
|
| Ec2MCS_like |
cd06108 |
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ... |
912-1077 |
6.21e-07 |
|
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: 53.08 E-value: 6.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 912 ICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKaFDSGIIPMEFVNKMKKEGKLIMGIGHRVKSINNPdmRVQIL 990
Cdd:cd06108 189 VTASTLSDFYSAITGAIGTLrGPLHGGANEAAMELIER-FKSPEEAEQGLLEKLERKELIMGFGHRVYKEGDP--RSDII 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 991 KDFVKQHFPATP---LLDYALEVEKITTSKKpNLILNVDGFIGVAFvdmlRNCG----SFTreeadeyvdigalnGIFVL 1063
Cdd:cd06108 266 KKWSKKLSEEGGdplLYQISERIEEVMWEEK-KLFPNLDFYSASAY----HFCGipteLFT--------------PIFVM 326
|
170
....*....|....
gi 313151222 1064 GRSMGFIGHYLDQK 1077
Cdd:cd06108 327 SRVTGWAAHIMEQR 340
|
|
| PRK14046 |
PRK14046 |
malate--CoA ligase subunit beta; Provisional |
185-402 |
8.67e-07 |
|
malate--CoA ligase subunit beta; Provisional
Pssm-ID: 237594 [Multi-domain] Cd Length: 392 Bit Score: 52.41 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 185 ISGLFNFYEDLYFTYLEINPLVVTKDGvYILDLAAKVDatadyickvkwgdiefpppFGREAYPEEAYIADLDAKS---- 260
Cdd:PRK14046 181 IMGCYRAFRDLDATMLEINPLVVTKDD-RVLALDAKMS-------------------FDDNALFRRPNIAEMRDPSqedp 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 261 ----GASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGvnELANYGEYSGAPSEQQTYDYAKTILSlmtrEKHPEGK 336
Cdd:PRK14046 241 reaqAAEHGLSYVGLDGDIGCIVNGAGLAMATMDMIKLAGG--EPANFLDVGGGASPERVAKAFRLVLS----DRNVKAI 314
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313151222 337 ILIIGGSIANFTNVAatfKGIVRAIRDYQgplkeHEVTIFVRRGGPNYQEGLRVMGEvgktTGIPI 402
Cdd:PRK14046 315 LVNIFAGINRCDWVA---EGVVQAAREVG-----IDVPLVVRLAGTNVEEGRKILAE----SGLPI 368
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
181-407 |
2.93e-06 |
|
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439815 [Multi-domain] Cd Length: 388 Bit Score: 50.82 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 181 LASFISGLFNFYEDLYFTYLEINPLVVTKDG-VYILDlaAKV--DATADY----IckVKWGDIEFPPPFGREAYPEE-AY 252
Cdd:COG0045 177 FAKILKKLYRAFVEKDASLVEINPLVVTKDGrLVALD--AKVnfDDNALFrhpeL--AALRDLSEEDPLEVEASKYGlNY 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 253 IAdLDaksgaslkltllnpkGRIWTMVAGGG---ASVvysDTICDLGGvnELANYGEYSGAPSEQQTYDYAKTILSlmtr 329
Cdd:COG0045 253 VK-LD---------------GNIGCMVNGAGlamATM---DIIKLAGG--EPANFLDVGGGATAERVAEAFKIILS---- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 330 ekHPEGK-ILI-IGGSIANFTNVAatfKGIVRAirdyqgpLKEHEVT--IFVRRGGPNYQEGLRVMGEvgktTGIPIHVF 405
Cdd:COG0045 308 --DPNVKaILVnIFGGITRCDVVA---EGIVAA-------LKEVGLKvpVVVRLEGTNVEEGRKILAE----SGLNIIAA 371
|
..
gi 313151222 406 GT 407
Cdd:COG0045 372 DT 373
|
|
| BSuCS-II_like |
cd06110 |
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ... |
888-1078 |
3.61e-06 |
|
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: 50.35 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 888 QFIEMCLMVTADHGPAVSgAHNTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKaFDSGIIPMEFVNKMKKE 966
Cdd:cd06110 168 RAFDVALILHADHELNAS-TFAARVVASTLSDMYSAVTAAIGALkGPLHGGANERVMKMLLE-IGSVDNVAAYVKDKLAN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 967 GKLIMGIGHRVksINNPDMRVQILKDFVKQ---HFPATPLLDYALEVEKITTSKKpNLILNVDGFIGVAFVDMlrncGsf 1043
Cdd:cd06110 246 KEKIMGFGHRV--YKTGDPRAKHLREMSRRlgkETGEPKWYEMSEAIEQAMRDEK-GLNPNVDFYSASVYYML----G-- 316
|
170 180 190
....*....|....*....|....*....|....*
gi 313151222 1044 treeadeyVDIGALNGIFVLGRSMGFIGHYLDQKR 1078
Cdd:cd06110 317 --------IPVDLFTPIFAISRVSGWCAHILEQYF 343
|
|
| PRK14035 |
PRK14035 |
citrate synthase; Provisional |
894-1078 |
1.05e-05 |
|
citrate synthase; Provisional
Pssm-ID: 184468 [Multi-domain] Cd Length: 371 Bit Score: 48.99 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 894 LMVTADHGPAVSgAHNTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKlIMG 972
Cdd:PRK14035 177 LVLHADHELNAS-TFTARCAVSSLSDMYSGVVAAVGSLkGPLHGGANERVMDMLSEIRSIGDVDAYLDEKFANKEK-IMG 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 973 IGHRVKSINNPdmRVQILKDFVKQHFPAT---PLLDYALEVEKITTSKKpNLILNVDGFIGVAFVDMLRNCGSFTReead 1049
Cdd:PRK14035 255 FGHRVYKDGDP--RAKYLREMSRKITKGTgreELFEMSVKIEKRMKEEK-GLIPNVDFYSATVYHVMGIPHDLFTP---- 327
|
170 180
....*....|....*....|....*....
gi 313151222 1050 eyvdigalngIFVLGRSMGFIGHYLDQKR 1078
Cdd:PRK14035 328 ----------IFAVSRVAGWIAHILEQYK 346
|
|
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
894-1079 |
1.00e-04 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 45.89 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 894 LMVTADHG-PAVSGAhnTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLIM 971
Cdd:PRK14037 177 LILYTDHEvPASTTA--ALVAASTLSDMYSCITAALAALkGPLHGGAAEEAFKQFVEIGDPNNVEMWFNDKIINGKKRLM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 972 GIGHRVKSINNPDMRV--QILKDFVKQHFPATPLLDYALEVEK--ITTSKKPNLILNVDGFIGVAFVDMLRNCGSFTree 1047
Cdd:PRK14037 255 GFGHRVYKTYDPRAKIfkELAETLIERNSEAKKYFEIAQKLEElgIKQFGSKGIYPNTDFYSGIVFYALGFPVYMFT--- 331
|
170 180 190
....*....|....*....|....*....|....*.
gi 313151222 1048 adeyvdigalnGIFVLGRSMGFIGHYL----DQKRL 1079
Cdd:PRK14037 332 -----------ALFALSRTLGWLAHIIeyveEQHRL 356
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
66-227 |
1.55e-04 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 45.47 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 66 RGKLGlvGVNL--SLDGVK----SWLKPRLGHEATVGKAKGFLKnFLIEPFVPhsQAEEFYVCIYATREGDYVLF--HHE 137
Cdd:PRK00696 54 RGKAG--GVKLakSPEEARefakQILGMTLVTHQTGPKGQPVNK-VLVEEGAD--IAKEYYLSIVLDRATRRVVFmaSTE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 138 GGVDVGDVDAKAQkllvgvdEKLNTEDIK----------RHLLVHA--PEDKKEVLASFISGLFNFYEDLYFTYLEINPL 205
Cdd:PRK00696 129 GGMDIEEVAEETP-------EKIHKVAIDpltglqpfqaREIAFKLglPGEQVKQFAKILMGLYKAFVEKDASLVEINPL 201
|
170 180
....*....|....*....|....*
gi 313151222 206 VVTKDG-VYILDlaAKV--DATADY 227
Cdd:PRK00696 202 VVTKDGdLIALD--AKInfDDNALF 224
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
890-996 |
1.77e-04 |
|
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: 45.34 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 890 IEMCLMVTADHGpavsGAHN----TIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMF-------SKAFDSGIIPm 957
Cdd:cd06113 198 LDLCLVLHAEHG----GGNNstftTRVVSSSGTDTYSAIAAAIGSLkGPRHGGANIKVMEMLedikenvKDWTDEDEVR- 272
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 313151222 958 EFVNKM--KKEGK---LIMGIGHRVKSINNPdmRVQILKDFVKQ 996
Cdd:cd06113 273 AYLRKIlnKEAFDksgLIYGMGHAVYTLSDP--RAVVLKKYARS 314
|
|
| PRK14036 |
PRK14036 |
citrate synthase; Provisional |
959-1076 |
2.87e-04 |
|
citrate synthase; Provisional
Pssm-ID: 237591 [Multi-domain] Cd Length: 377 Bit Score: 44.56 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 959 FVNKMKKEGKLIMGIGHRVKSINNPdmRVQILKDFVKQ---HFPATPLLDYALEVEKITTSK-KPNLIL-NVDGFIGVAF 1033
Cdd:PRK14036 243 YLDERLANKQKIMGFGHREYKVKDP--RATILQKLAEElfaRFGHDEYYEIALELERVAEERlGPKGIYpNVDFYSGLVY 320
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 313151222 1034 VDMLRNCGSFTreeadeyvdigalnGIFVLGRSMGFIGHYLDQ 1076
Cdd:PRK14036 321 RKLGIPRDLFT--------------PIFAIARVAGWLAHWREQ 349
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
6-207 |
2.62e-03 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 40.32 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 6 ISEQTGKELLYKYICTTSaiqnRFKYARvTPDT--DWAHLLQDHPWllsqslVVKPDQLIKRRGKLGLVGVNLSLDGVKS 83
Cdd:pfam08442 2 LHEYQAKEIFAKYGIPVP----RGEVAT-SPEEaeEIAKKLGGKVY------VVKAQVLAGGRGKAGGVKLAKSPEEAKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151222 84 WLKPRLGHE---ATVGKAKGFLKNFLIEPFVPhsQAEEFYVCIYATRE--GDYVLFHHEGGVDVGDVDAKAQKLL--VGV 156
Cdd:pfam08442 71 VAKEMLGKNlvtKQTGPDGQPVNKVLVEEALD--IKKEYYLSIVLDRAskGPVIIASTEGGVDIEEVAAKNPEKIhkFPI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 313151222 157 DEKLN-TEDIKRHLLVHA--PEDKKEVLASFISGLFNFYEDLYFTYLEINPLVV 207
Cdd:pfam08442 149 DPLKGlTPYQAREIAFKLglPGELIKQAADIIKKLYKLFVEYDATLVEINPLVE 202
|
|
| |
