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Conserved domains on  [gi|491993603|ref|WP_005710674|]
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phosphogluconate dehydrogenase (NAD(+)-dependent, decarboxylating) [Lacticaseibacillus rhamnosus]

Protein Classification

decarboxylating 6-phosphogluconate dehydrogenase( domain architecture ID 11484385)

NADP-dependent decarboxylating 6-phosphogluconate dehydrogenase (6-PGDH) catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NAD to NADH

CATH:  3.40.50.720
EC:  1.1.1.-
Gene Ontology:  GO:0004616|GO:0050661

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
29-324 0e+00

NADP-dependent phosphogluconate dehydrogenase;


:

Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 519.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  29 MQVGMVGLGKMGMNLVANMRDHDIEVVAFDLNDQARTEVGKYQVKAVASLDALVMSLASPRIIWSMVPAGKPTAATIQQL 108
Cdd:PRK09599   1 MQLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPAPRVVWLMVPAGEITDATIDEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 109 AKLLSPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGARANGNFMIGGDEDQFAQIEPLFKAIA--APSGY 186
Cdd:PRK09599  81 APLLSPGDIVIDGGNSYYKDDIRRAELLAEKGIHFVDVGTSGGVWGLERGYCLMIGGDKEAVERLEPIFKALAprAEDGY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 187 LYTGPVGSGHYLKMVHNGIEYGMMQAIGEGFDVLAHSPYAYDNAAVAKMWNHGSVIRSWLMELAGDAFSEDADLAKIQGI 266
Cdd:PRK09599 161 LHAGPVGAGHFVKMVHNGIEYGMMQAYAEGFELLEASRFDLDLAAVAEVWRRGSVIRSWLLDLTADALAEDPKLDEISGY 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491993603 267 MHSSGEGAWTVEEALRLHVATPVIASALMMRYRSEEADTMTGKVVAALRNQFGGHAVD 324
Cdd:PRK09599 241 VEDSGEGRWTVEEAIDLAVPAPVIAAALFMRFRSRQEDSFADKVVAALRNGFGGHAVK 298
 
Name Accession Description Interval E-value
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
29-324 0e+00

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 519.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  29 MQVGMVGLGKMGMNLVANMRDHDIEVVAFDLNDQARTEVGKYQVKAVASLDALVMSLASPRIIWSMVPAGKPTAATIQQL 108
Cdd:PRK09599   1 MQLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPAPRVVWLMVPAGEITDATIDEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 109 AKLLSPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGARANGNFMIGGDEDQFAQIEPLFKAIA--APSGY 186
Cdd:PRK09599  81 APLLSPGDIVIDGGNSYYKDDIRRAELLAEKGIHFVDVGTSGGVWGLERGYCLMIGGDKEAVERLEPIFKALAprAEDGY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 187 LYTGPVGSGHYLKMVHNGIEYGMMQAIGEGFDVLAHSPYAYDNAAVAKMWNHGSVIRSWLMELAGDAFSEDADLAKIQGI 266
Cdd:PRK09599 161 LHAGPVGAGHFVKMVHNGIEYGMMQAYAEGFELLEASRFDLDLAAVAEVWRRGSVIRSWLLDLTADALAEDPKLDEISGY 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491993603 267 MHSSGEGAWTVEEALRLHVATPVIASALMMRYRSEEADTMTGKVVAALRNQFGGHAVD 324
Cdd:PRK09599 241 VEDSGEGRWTVEEAIDLAVPAPVIAAALFMRFRSRQEDSFADKVVAALRNGFGGHAVK 298
YqeC COG1023
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
29-323 0e+00

6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];


Pssm-ID: 440646 [Multi-domain]  Cd Length: 300  Bit Score: 517.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  29 MQVGMVGLGKMGMNLVANMRDHDIEVVAFDLNDQARTEVGKYQVKAVASLDALVMSLASPRIIWSMVPAGKPTAATIQQL 108
Cdd:COG1023    1 MQIGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKLPAPRVVWLMVPAGEITDQVIEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 109 AKLLSPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGARANGNFMIGGDEDQFAQIEPLFKAIA--APSGY 186
Cdd:COG1023   81 APLLEPGDIVIDGGNSNYKDDIRRAEELAEKGIHFVDVGTSGGVWGLENGYCLMIGGDKEAVERLEPIFKALApgAENGY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 187 LYTGPVGSGHYLKMVHNGIEYGMMQAIGEGFDVLAHSPYAYDNAAVAKMWNHGSVIRSWLMELAGDAFSEDADLAKIQGI 266
Cdd:COG1023  161 LHCGPVGAGHFVKMVHNGIEYGMMQAYAEGFELLEASEFDLDLAEVAEVWRRGSVIRSWLLDLTADALAEDPKLEGISGY 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491993603 267 MHSSGEGAWTVEEALRLHVATPVIASALMMRYRSEEADTMTGKVVAALRNQFGGHAV 323
Cdd:COG1023  241 VEDSGEGRWTVEEAIELGVPAPVITAALFARFRSRQEDSFADKVLAALRNQFGGHAV 297
gnd_rel TIGR00872
6-phosphogluconate dehydrogenase (decarboxylating); This family resembles a larger family (gnd) ...
 29-323 6.47e-124

6-phosphogluconate dehydrogenase (decarboxylating); This family resembles a larger family (gnd) of bacterial and eukaryotic 6-phosphogluconate dehydrogenases but differs from it by a deep split in a UPGMA similarity clustering tree and the lack of a central region of about 140 residues. Among complete genomes, it is found is found in Bacillus subtilis and Mycobacterium tuberculosis, both of which also contain gnd, and in Aquifex aeolicus. The protein from Methylobacillus flagellatus KT has been characterized as a decarboxylating 6-phosphogluconate dehydrogenase as part of an unusual formaldehyde oxidation cycle. In some sequenced organisms members of this family are the sole 6-phosphogluconate dehydrogenase present and are probably active in the pentose phosphate cycle. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 273313 [Multi-domain]  Cd Length: 298  Bit Score: 357.23  E-value: 6.47e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603   29 MQVGMVGLGKMGMNLVANMRDHDIEVVAFDLNDQARTEVGKYQVKAVASLDALVMSLASPRIIWSMVPAGKpTAATIQQL 108
Cdd:TIGR00872   1 MQLGLIGLGRMGANIVRRLAKRGHDCVGYDHDQDAVKAMKEDRTTGVANLRELSQRLSAPRVVWVMVPHGI-VDAVLEEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  109 AKLLSPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGARANGNFMIGGDEDQFAQIEPLFKAIA-APSGYL 187
Cdd:TIGR00872  80 APTLEKGDIVIDGGNSYYKDSLRRYKLLKEKGIHLLDCGTSGGVWGRERGYCFMIGGDGEAFARAEPLFADVApEEQGYL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  188 YTGPVGSGHYLKMVHNGIEYGMMQAIGEGFDVLAHSPYAYDNAAVAKMWNHGSVIRSWLMELAGDAFSEDADLAKIQGIM 267
Cdd:TIGR00872 160 YCGPCGSGHFVKMVHNGIEYGMMAAIAEGFEILRNSQFDFDIPEVARVWRRGSVIRSWLLDLTAIAFRESPDLAEFSGRV 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 491993603  268 HSSGEGAWTVEEALRLHVATPVIASALMMRYRSEEADTMTGKVVAALRNQFGGHAV 323
Cdd:TIGR00872 240 SDSGEGRWTVIAAIDLGVPAPVIATSLQSRFASRDLDDFANKVLAALRKEFGGHAE 295
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 30-182 5.86e-41

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 140.30  E-value: 5.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603   30 QVGMVGLGKMGMNLVANMRDHDIEVVAFDLNDQARTEVGKYQVKAVASLDALVMSLaspRIIWSMVPAGKPTAATIQQ-- 107
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGL---DVVITMVPAGAAVDAVIFGeg 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491993603  108 LAKLLSPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGARaNG--NFMIGGDEDQFAQIEPLFKAIAA 182
Cdd:pfam03446  78 LLPGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAE-NGtlSIMVGGDEEAFERVKPILEAMGA 153
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 11-115 5.56e-03

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 38.00  E-value: 5.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  11 DArvVATPAHA--HAQEV-ANMQVGMVGLGKMGMNLVANMRDHDIEVVAFDLNDQARTEVGKYQV-KAVASLD---ALVM 83
Cdd:cd08254  148 DA--VLTPYHAvvRAGEVkPGETVLVIGLGGLGLNAVQIAKAMGAAVIAVDIKEEKLELAKELGAdEVLNSLDdspKDKK 225

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491993603  84 SLASPRIIWSMVP-AGkpTAATIQQLAKLLSPG 115
Cdd:cd08254  226 AAGLGGGFDVIFDfVG--TQPTFEDAQKAVKPG 256
 
Name Accession Description Interval E-value
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
29-324 0e+00

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 519.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  29 MQVGMVGLGKMGMNLVANMRDHDIEVVAFDLNDQARTEVGKYQVKAVASLDALVMSLASPRIIWSMVPAGKPTAATIQQL 108
Cdd:PRK09599   1 MQLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPAPRVVWLMVPAGEITDATIDEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 109 AKLLSPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGARANGNFMIGGDEDQFAQIEPLFKAIA--APSGY 186
Cdd:PRK09599  81 APLLSPGDIVIDGGNSYYKDDIRRAELLAEKGIHFVDVGTSGGVWGLERGYCLMIGGDKEAVERLEPIFKALAprAEDGY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 187 LYTGPVGSGHYLKMVHNGIEYGMMQAIGEGFDVLAHSPYAYDNAAVAKMWNHGSVIRSWLMELAGDAFSEDADLAKIQGI 266
Cdd:PRK09599 161 LHAGPVGAGHFVKMVHNGIEYGMMQAYAEGFELLEASRFDLDLAAVAEVWRRGSVIRSWLLDLTADALAEDPKLDEISGY 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491993603 267 MHSSGEGAWTVEEALRLHVATPVIASALMMRYRSEEADTMTGKVVAALRNQFGGHAVD 324
Cdd:PRK09599 241 VEDSGEGRWTVEEAIDLAVPAPVIAAALFMRFRSRQEDSFADKVVAALRNGFGGHAVK 298
YqeC COG1023
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
29-323 0e+00

6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];


Pssm-ID: 440646 [Multi-domain]  Cd Length: 300  Bit Score: 517.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  29 MQVGMVGLGKMGMNLVANMRDHDIEVVAFDLNDQARTEVGKYQVKAVASLDALVMSLASPRIIWSMVPAGKPTAATIQQL 108
Cdd:COG1023    1 MQIGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKLPAPRVVWLMVPAGEITDQVIEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 109 AKLLSPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGARANGNFMIGGDEDQFAQIEPLFKAIA--APSGY 186
Cdd:COG1023   81 APLLEPGDIVIDGGNSNYKDDIRRAEELAEKGIHFVDVGTSGGVWGLENGYCLMIGGDKEAVERLEPIFKALApgAENGY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 187 LYTGPVGSGHYLKMVHNGIEYGMMQAIGEGFDVLAHSPYAYDNAAVAKMWNHGSVIRSWLMELAGDAFSEDADLAKIQGI 266
Cdd:COG1023  161 LHCGPVGAGHFVKMVHNGIEYGMMQAYAEGFELLEASEFDLDLAEVAEVWRRGSVIRSWLLDLTADALAEDPKLEGISGY 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491993603 267 MHSSGEGAWTVEEALRLHVATPVIASALMMRYRSEEADTMTGKVVAALRNQFGGHAV 323
Cdd:COG1023  241 VEDSGEGRWTVEEAIELGVPAPVITAALFARFRSRQEDSFADKVLAALRNQFGGHAV 297
gnd_rel TIGR00872
6-phosphogluconate dehydrogenase (decarboxylating); This family resembles a larger family (gnd) ...
 29-323 6.47e-124

6-phosphogluconate dehydrogenase (decarboxylating); This family resembles a larger family (gnd) of bacterial and eukaryotic 6-phosphogluconate dehydrogenases but differs from it by a deep split in a UPGMA similarity clustering tree and the lack of a central region of about 140 residues. Among complete genomes, it is found is found in Bacillus subtilis and Mycobacterium tuberculosis, both of which also contain gnd, and in Aquifex aeolicus. The protein from Methylobacillus flagellatus KT has been characterized as a decarboxylating 6-phosphogluconate dehydrogenase as part of an unusual formaldehyde oxidation cycle. In some sequenced organisms members of this family are the sole 6-phosphogluconate dehydrogenase present and are probably active in the pentose phosphate cycle. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 273313 [Multi-domain]  Cd Length: 298  Bit Score: 357.23  E-value: 6.47e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603   29 MQVGMVGLGKMGMNLVANMRDHDIEVVAFDLNDQARTEVGKYQVKAVASLDALVMSLASPRIIWSMVPAGKpTAATIQQL 108
Cdd:TIGR00872   1 MQLGLIGLGRMGANIVRRLAKRGHDCVGYDHDQDAVKAMKEDRTTGVANLRELSQRLSAPRVVWVMVPHGI-VDAVLEEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  109 AKLLSPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGARANGNFMIGGDEDQFAQIEPLFKAIA-APSGYL 187
Cdd:TIGR00872  80 APTLEKGDIVIDGGNSYYKDSLRRYKLLKEKGIHLLDCGTSGGVWGRERGYCFMIGGDGEAFARAEPLFADVApEEQGYL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  188 YTGPVGSGHYLKMVHNGIEYGMMQAIGEGFDVLAHSPYAYDNAAVAKMWNHGSVIRSWLMELAGDAFSEDADLAKIQGIM 267
Cdd:TIGR00872 160 YCGPCGSGHFVKMVHNGIEYGMMAAIAEGFEILRNSQFDFDIPEVARVWRRGSVIRSWLLDLTAIAFRESPDLAEFSGRV 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 491993603  268 HSSGEGAWTVEEALRLHVATPVIASALMMRYRSEEADTMTGKVVAALRNQFGGHAV 323
Cdd:TIGR00872 240 SDSGEGRWTVIAAIDLGVPAPVIATSLQSRFASRDLDDFANKVLAALRKEFGGHAE 295
Gnd COG0362
6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate ...
 27-300 6.67e-80

6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate dehydrogenase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 440131 [Multi-domain]  Cd Length: 467  Bit Score: 250.76  E-value: 6.67e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  27 ANMQVGMVGLGKMGMNLVANMRDHDIEVVAFDLnDQART-----EVGKYQ-VKAVASLDALVMSLASPRIIWSMVPAGKP 100
Cdd:COG0362    1 AKADIGVIGLAVMGRNLALNIADHGFSVAVYNR-TAEKTdaflaEHGKGKnIVGTYSLEEFVASLERPRKILLMVKAGKP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 101 TAATIQQLAKLLSPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGARaNG-NFMIGGDEDQFAQIEPLFKA 179
Cdd:COG0362   80 VDAVIEQLLPLLEPGDIIIDGGNSHFTDTIRREKELAEKGIHFIGMGVSGGEEGAL-HGpSIMPGGSKEAYELVKPILEA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 180 IAAPSGYL----YTGPVGSGHYLKMVHNGIEYGMMQAIGEGFDVLAHSpYAYDNAAVAKM---WNHGsVIRSWLMELAGD 252
Cdd:COG0362  159 IAAKVDGEpcvtYIGPDGAGHFVKMVHNGIEYADMQLIAEAYDLLRDG-LGLSNDEIAEVfaeWNKG-ELDSYLIEITAD 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491993603 253 AFSE-DADLAK--IQGIMHSSGE---GAWTVEEALRLHVATPVIASALMMRYRS 300
Cdd:COG0362  237 ILRKkDPETGKplVDVILDKAGQkgtGKWTSQSALDLGVPLPLITEAVFARYLS 290
PRK09287 PRK09287
NADP-dependent phosphogluconate dehydrogenase;
39-300 9.32e-69

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236453 [Multi-domain]  Cd Length: 459  Bit Score: 221.54  E-value: 9.32e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  39 MGMNLVANMRDHDIEVVAFDLnDQARTE------VGKYQVKAVASLDALVMSLASPRIIWSMVPAGKPTAATIQQLAKLL 112
Cdd:PRK09287   1 MGKNLALNIASHGYTVAVYNR-TPEKTDeflaeeGKGKKIVPAYTLEEFVASLEKPRKILLMVKAGAPVDAVIEQLLPLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 113 SPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGARaNG-NFMIGGDEDQFAQIEPLFKAIAA--PSGY--- 186
Cdd:PRK09287  80 EKGDIIIDGGNSNYKDTIRREKELAEKGIHFIGMGVSGGEEGAL-HGpSIMPGGQKEAYELVAPILEKIAAkvEDGEpcv 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 187 LYTGPVGSGHYLKMVHNGIEYGMMQAIGEGFDVLAHSpYAYDNAAVAKM---WNHGSViRSWLMELAGDAFS-EDAD--- 259
Cdd:PRK09287 159 TYIGPDGAGHYVKMVHNGIEYGDMQLIAEAYDLLKDG-LGLSAEEIADVfaeWNKGEL-NSYLIEITADILRqKDEEtgk 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 491993603 260 --LAKIQGIMHSSGEGAWTVEEALRLHVATPVIASALMMRYRS 300
Cdd:PRK09287 237 plVDVILDKAGQKGTGKWTSQSALDLGVPLTLITEAVFARYLS 279
gnd TIGR00873
6-phosphogluconate dehydrogenase (decarboxylating); This model does not specify whether the ...
 30-300 1.26e-68

6-phosphogluconate dehydrogenase (decarboxylating); This model does not specify whether the cofactor is NADP only (EC 1.1.1.44), NAD only, or both. The model does not assign an EC number for that reason. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 273314 [Multi-domain]  Cd Length: 467  Bit Score: 221.51  E-value: 1.26e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603   30 QVGMVGLGKMGMNLVANMRDHDIEVVAF----DLNDQARTEVGKYQ-VKAVASLDALVMSLASPRIIWSMVPAGKPTAAT 104
Cdd:TIGR00873   1 DIGVIGLAVMGQNLALNMEDHGFTVSVYnrtpSKTDEFLAEEAKGKsIIGAYSIEDFVQSLERPRKIMLMVKAGAPVDAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  105 IQQLAKLLSPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGARANGNFMIGGDEDQFAQIEPLFKAIAAPS 184
Cdd:TIGR00873  81 IDSLLPLLEKGDIIIDGGNSHYPDTERRYKELKAKGILFVGSGVSGGEEGARKGPSIMPGGSPEAWPLVAPIFQSIAAKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  185 G----YLYTGPVGSGHYLKMVHNGIEYGMMQAIGEGFDVLAHS-PYAYDN-AAVAKMWNHGsVIRSWLMELAGDAFS-ED 257
Cdd:TIGR00873 161 DgepcCTWVGPGGAGHYVKMVHNGIEYGDMQLICEAYDILKRGlGLSNEEiAEIFTEWNNG-ELDSYLIEITADILAkKD 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 491993603  258 AD----LAKIQGIMHSSGEGAWTVEEALRLHVATPVIASALMMRYRS 300
Cdd:TIGR00873 240 EDgnplVDKILDTAGQKGTGKWTAINALDLGVPLTLITESVFARYLS 286
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 31-300 2.29e-63

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 208.10  E-value: 2.29e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  31 VGMVGLGKMGMNLVANMRDHDIEVVAFDlNDQARTEV-------GKYQVKAVASLDALVMSLASPRIIWSMVPAGKPTAA 103
Cdd:PTZ00142   4 IGLIGLAVMGQNLALNIASRGFKISVYN-RTYEKTEEfvkkakeGNTRVKGYHTLEELVNSLKKPRKVILLIKAGEAVDE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 104 TIQQLAKLLSPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGARANGNFMIGGDEDQFAQIEPLFKAIAAP 183
Cdd:PTZ00142  83 TIDNLLPLLEKGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGPSLMPGGNKEAYDHVKDILEKCSAK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 184 SG----YLYTGPVGSGHYLKMVHNGIEYGMMQAIGEGFDVLAHSpYAYDN---AAVAKMWNHGsVIRSWLMELAGDAFSE 256
Cdd:PTZ00142 163 VGdspcVTYVGPGSSGHYVKMVHNGIEYGDMQLISESYKLMKHI-LGMSNeelSEVFNKWNEG-ILNSYLIEITAKILAK 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 491993603 257 DADLA------KIQGIMHSSGEGAWTVEEALRLHVATPVIASALMMRYRS 300
Cdd:PTZ00142 241 KDDLGeehlvdKILDIAGSKGTGKWTVQEALERGIPVPTMAASVDARNIS 290
PLN02350 PLN02350
phosphogluconate dehydrogenase (decarboxylating)
 30-300 8.13e-58

phosphogluconate dehydrogenase (decarboxylating)


Pssm-ID: 215200 [Multi-domain]  Cd Length: 493  Bit Score: 194.16  E-value: 8.13e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  30 QVGMVGLGKMGMNLVANMRDHDIEVVAFDLN--------DQARTEvGKYQVKAVASLDALVMSLASPRIIWSMVPAGKPT 101
Cdd:PLN02350   8 RIGLAGLAVMGQNLALNIAEKGFPISVYNRTtskvdetvERAKKE-GNLPLYGFKDPEDFVLSIQKPRSVIILVKAGAPV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 102 AATIQQLAKLLSPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGARANGNFMIGGDEDQFAQIEPLFKAIA 181
Cdd:PLN02350  87 DQTIKALSEYMEPGDCIIDGGNEWYENTERRIKEAAEKGLLYLGMGVSGGEEGARNGPSLMPGGSFEAYKNIEDILEKVA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 182 AP--SG--YLYTGPVGSGHYLKMVHNGIEYGMMQAIGEGFDVLaHSPYAYDN---AAVAKMWNHGSvIRSWLMELAGDAF 254
Cdd:PLN02350 167 AQvdDGpcVTYIGPGGAGNFVKMVHNGIEYGDMQLISEAYDVL-KSVGGLSNeelAEVFAEWNKGE-LESFLIEITADIF 244

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491993603 255 SEDADLA------KIQGIMHSSGEGAWTVEEALRLHVATPVIASALMMRYRS 300
Cdd:PLN02350 245 SVKDDKGdgylvdKILDKTGMKGTGKWTVQQAAELSVAAPTIAASLDARYLS 296
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 30-182 5.86e-41

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 140.30  E-value: 5.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603   30 QVGMVGLGKMGMNLVANMRDHDIEVVAFDLNDQARTEVGKYQVKAVASLDALVMSLaspRIIWSMVPAGKPTAATIQQ-- 107
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGL---DVVITMVPAGAAVDAVIFGeg 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491993603  108 LAKLLSPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGARaNG--NFMIGGDEDQFAQIEPLFKAIAA 182
Cdd:pfam03446  78 LLPGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAE-NGtlSIMVGGDEEAFERVKPILEAMGA 153
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 29-253 2.88e-28

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 110.59  E-value: 2.88e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  29 MQVGMVGLGKMGMNLVANMRDHDIEVVAFDLNDQARTEVGKYQVKAVASLDALVmslASPRIIWSMVPAGKPTAATI--- 105
Cdd:COG2084    2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAA---AAADVVITMLPDDAAVEEVLlge 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 106 QQLAKLLSPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGARA-NGNFMIGGDEDQFAQIEPLFKAIAapS 184
Cdd:COG2084   79 DGLLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAgTLTIMVGGDEAAFERARPVLEAMG--K 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491993603 185 GYLYTGPVGSGHYLKMVHNGIEYGMMQAIGEGFdVLAHSpYAYDNAAVAKMWNHGSViRSWLMELAGDA 253
Cdd:COG2084  157 RIVHVGDAGAGQAAKLANNLLLAGTMAALAEAL-ALAEK-AGLDPETLLEVLSGGAA-GSWVLENRGPR 222
6PGD pfam00393
6-phosphogluconate dehydrogenase, C-terminal domain; This family represents the C-terminal ...
 195-300 9.74e-25

6-phosphogluconate dehydrogenase, C-terminal domain; This family represents the C-terminal all-alpha domain of 6-phosphogluconate dehydrogenase. The domain contains two structural repeats of 5 helices each.


Pssm-ID: 459797  Cd Length: 290  Bit Score: 101.38  E-value: 9.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  195 GHYLKMVHNGIEYGMMQAIGEGFDVLAHSpYAYDNAAVA---KMWNHGsVIRSWLMELAGDAFSE-DADLAK--IQGIMH 268
Cdd:pfam00393   1 GHYVKMVHNGIEYGDMQLIAEAYDLLKRG-LGLSNDEIAdvfEEWNKG-ELDSYLIEITADILRKkDPEDGKplVDKILD 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 491993603  269 SSGE---GAWTVEEALRLHVATPVIASALMMRYRS 300
Cdd:pfam00393  79 KAGQkgtGKWTVQEALDLGVPAPTIAEAVFARCLS 113
garR PRK11559
tartronate semialdehyde reductase; Provisional
 29-221 3.03e-14

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 72.01  E-value: 3.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  29 MQVGMVGLGKMGMNLVANMRDHDIEVVAFDLNDQARTEVGKYQVKAVASLDAlvMSLASPRIIwSMVPAGKPTAATI--- 105
Cdd:PRK11559   3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKA--VAEQCDVII-TMLPNSPHVKEVAlge 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 106 QQLAKLLSPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGArANGN--FMIGGDEDQFAQIEPLFKAIAAP 183
Cdd:PRK11559  80 NGIIEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKA-IDGTlsVMVGGDKAIFDKYYDLMKAMAGS 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 491993603 184 SgyLYTGPVGSGHYLKMVHNGIEYGMMQAIGEGFdVLA 221
Cdd:PRK11559 159 V--VHTGDIGAGNVTKLANQVIVALNIAAMSEAL-VLA 193
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
29-217 3.09e-04

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 41.93  E-value: 3.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  29 MQVGMVGLGKMGMNLVANMRD--HDIEVVAFDLNDQARTEVGKYQVKAVASLDAlvmslaSPRIIWSMVPAGKPTAATI- 105
Cdd:PRK15059   1 MKLGFIGLGIMGTPMAINLARagHQLHVTTIGPVADELLSLGAVSVETARQVTE------ASDIIFIMVPDTPQVEEVLf 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 106 --QQLAKLLSPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGARANG-NFMIGGDEDQFAQIEPLFKAIAa 182
Cdd:PRK15059  75 geNGCTKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTlSIMVGGDEAVFERVKPLFELLG- 153

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 491993603 183 pSGYLYTGPVGSGHYLKMVHNGIEYGMMQAIGEGF 217
Cdd:PRK15059 154 -KNITLVGGNGDGQTCKVANQIIVALNIEAVSEAL 187
MviM COG0673
Predicted dehydrogenase [General function prediction only];
29-90 3.92e-04

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 41.45  E-value: 3.92e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491993603  29 MQVGMVGLGKMGMNLVANMRDH-DIEVVA-FDLNDQARTEVG-KYQVKAVASLDALvmsLASPRI 90
Cdd:COG0673    4 LRVGIIGAGGIGRAHAPALAALpGVELVAvADRDPERAEAFAeEYGVRVYTDYEEL---LADPDI 65
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
31-203 3.21e-03

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 38.68  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  31 VGMVGLGKMGMNLVANMRDHDIEVVAFDLNDQA-RTEVGKYQVKAVASLDAlvmsLASPRIIWSMVPAGKPTAATI---Q 106
Cdd:PRK15461   4 IAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAvDALVDKGATPAASPAQA----AAGAEFVITMLPNGDLVRSVLfgeN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603 107 QLAKLLSPGDVVIDGGNSYYQDSIAHGKLLAAEGIHFFDVGTSGGMAGARAnGNFMI--GGDEDQFAQIEPLFKAIAapS 184
Cdd:PRK15461  80 GVCEGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAIT-GTLLLlaGGTAEQVERATPILMAMG--N 156

                        170
                 ....*....|....*....
gi 491993603 185 GYLYTGPVGSGHYLKMVHN 203
Cdd:PRK15461 157 ELINAGGPGMGIRVKLINN 175
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 11-115 5.56e-03

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 38.00  E-value: 5.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603  11 DArvVATPAHA--HAQEV-ANMQVGMVGLGKMGMNLVANMRDHDIEVVAFDLNDQARTEVGKYQV-KAVASLD---ALVM 83
Cdd:cd08254  148 DA--VLTPYHAvvRAGEVkPGETVLVIGLGGLGLNAVQIAKAMGAAVIAVDIKEEKLELAKELGAdEVLNSLDdspKDKK 225

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491993603  84 SLASPRIIWSMVP-AGkpTAATIQQLAKLLSPG 115
Cdd:cd08254  226 AAGLGGGFDVIFDfVG--TQPTFEDAQKAVKPG 256
PLN02858 PLN02858
fructose-bisphosphate aldolase
 1-202 7.25e-03

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 38.29  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603    1 MVDSLVQKLIDARVVATPAHAHAQEVAnmQVGMVGLGKMGMNLVANMRDHDIEVVAFDLNDQARTE-------VGKYQVK 73
Cdd:PLN02858  299 ILEAANRELYKPEDLAKQITMQAKPVK--RIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRfenagglAGNSPAE 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993603   74 AVASLDALVMSLASPRIIWSM-------VPAGKPTAATIqqLAKLLSPGDVvidggnsyyqdsIAHGKLLAAE--GIHFF 144
Cdd:PLN02858  377 VAKDVDVLVIMVANEVQAENVlfgdlgaVSALPAGASIV--LSSTVSPGFV------------IQLERRLENEgrDIKLV 442

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491993603  145 DVGTSGGMAGArANGNFMI---GGDEdqfaQIEPLFKAIAAPSGYLYT--GPVGSGHYLKMVH 202
Cdd:PLN02858  443 DAPVSGGVKRA-AMGTLTImasGTDE----ALKSAGSVLSALSEKLYVikGGCGAGSGVKMVN 500
 
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.
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