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Conserved domains on  [gi|446688635|ref|WP_000765981|]
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MULTISPECIES: phosphogluconate dehydrogenase (NAD(+)-dependent, decarboxylating) [Bacillus]

Protein Classification

NADP(+)-dependent, decarboxylating phosphogluconate dehydrogenase( domain architecture ID 11436990)

NADP(+)-dependent decarboxylating phosphogluconate dehydrogenase catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate, as part of the oxidative branch of the pentose phosphate pathway

CATH:  3.40.50.720|1.20.5.320
EC:  1.1.1.44
Gene Ontology:  GO:0004616|GO:0050661|GO:0006098|GO:0046177
PubMed:  35234135|34709178|26479318
SCOP:  3000048

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YqeC COG1023
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
1-298 0e+00

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


:

Pssm-ID: 440646 [Multi-domain]  Cd Length: 300  Bit Score: 545.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   1 MKLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVEKAGKLGITARHTLKEMIAELEAPRTIWVMVPAGEVVESVLKDV 80
Cdd:COG1023    1 MQIGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKLPAPRVVWLMVPAGEITDQVIEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  81 YPLLDEGDIVIEGGNSFYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGACLMVGGEKEIYDQLEPLFKDLAV--ENGY 158
Cdd:COG1023   81 APLLEPGDIVIDGGNSNYKDDIRRAEELAEKGIHFVDVGTSGGVWGLENGYCLMIGGDKEAVERLEPIFKALAPgaENGY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635 159 SYAGRVGSGHFLKMVHNGIEYGMMQAIAEGFEVLDKSDFDFNYEDVAKVWANGSVIRGWLMDLTEKAFADDPKLDGIKGV 238
Cdd:COG1023  161 LHCGPVGAGHFVKMVHNGIEYGMMQAYAEGFELLEASEFDLDLAEVAEVWRRGSVIRSWLLDLTADALAEDPKLEGISGY 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635 239 MNSSGEGKWTVETALELQAAAPVIAMSLFMRYRSQEDDTFHGKVVSALRNQFGGHEVVKK 298
Cdd:COG1023  241 VEDSGEGRWTVEEAIELGVPAPVITAALFARFRSRQEDSFADKVLAALRNQFGGHAVKKK 300
 
Name Accession Description Interval E-value
YqeC COG1023
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
1-298 0e+00

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


Pssm-ID: 440646 [Multi-domain]  Cd Length: 300  Bit Score: 545.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   1 MKLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVEKAGKLGITARHTLKEMIAELEAPRTIWVMVPAGEVVESVLKDV 80
Cdd:COG1023    1 MQIGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKLPAPRVVWLMVPAGEITDQVIEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  81 YPLLDEGDIVIEGGNSFYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGACLMVGGEKEIYDQLEPLFKDLAV--ENGY 158
Cdd:COG1023   81 APLLEPGDIVIDGGNSNYKDDIRRAEELAEKGIHFVDVGTSGGVWGLENGYCLMIGGDKEAVERLEPIFKALAPgaENGY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635 159 SYAGRVGSGHFLKMVHNGIEYGMMQAIAEGFEVLDKSDFDFNYEDVAKVWANGSVIRGWLMDLTEKAFADDPKLDGIKGV 238
Cdd:COG1023  161 LHCGPVGAGHFVKMVHNGIEYGMMQAYAEGFELLEASEFDLDLAEVAEVWRRGSVIRSWLLDLTADALAEDPKLEGISGY 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635 239 MNSSGEGKWTVETALELQAAAPVIAMSLFMRYRSQEDDTFHGKVVSALRNQFGGHEVVKK 298
Cdd:COG1023  241 VEDSGEGRWTVEEAIELGVPAPVITAALFARFRSRQEDSFADKVLAALRNQFGGHAVKKK 300
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
1-298 0e+00

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 530.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   1 MKLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVEKAGKLGITARHTLKEMIAELEAPRTIWVMVPAGEVVESVLKDV 80
Cdd:PRK09599   1 MQLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPAPRVVWLMVPAGEITDATIDEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  81 YPLLDEGDIVIEGGNSFYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGACLMVGGEKEIYDQLEPLFKDLAV--ENGY 158
Cdd:PRK09599  81 APLLSPGDIVIDGGNSYYKDDIRRAELLAEKGIHFVDVGTSGGVWGLERGYCLMIGGDKEAVERLEPIFKALAPraEDGY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635 159 SYAGRVGSGHFLKMVHNGIEYGMMQAIAEGFEVLDKSDFDFNYEDVAKVWANGSVIRGWLMDLTEKAFADDPKLDGIKGV 238
Cdd:PRK09599 161 LHAGPVGAGHFVKMVHNGIEYGMMQAYAEGFELLEASRFDLDLAAVAEVWRRGSVIRSWLLDLTADALAEDPKLDEISGY 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635 239 MNSSGEGKWTVETALELQAAAPVIAMSLFMRYRSQEDDTFHGKVVSALRNQFGGHEVVKK 298
Cdd:PRK09599 241 VEDSGEGRWTVEEAIDLAVPAPVIAAALFMRFRSRQEDSFADKVVAALRNGFGGHAVKKK 300
gnd_rel TIGR00872
6-phosphogluconate dehydrogenase (decarboxylating); This family resembles a larger family (gnd) ...
 1-298 6.07e-138

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: 391.52  E-value: 6.07e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635    1 MKLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVEKAGKLGITARHTLKEMIAELEAPRTIWVMVPAGeVVESVLKDV 80
Cdd:TIGR00872   1 MQLGLIGLGRMGANIVRRLAKRGHDCVGYDHDQDAVKAMKEDRTTGVANLRELSQRLSAPRVVWVMVPHG-IVDAVLEEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   81 YPLLDEGDIVIEGGNSFYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGACLMVGGEKEIYDQLEPLFKDLAVEN-GYS 159
Cdd:TIGR00872  80 APTLEKGDIVIDGGNSYYKDSLRRYKLLKEKGIHLLDCGTSGGVWGRERGYCFMIGGDGEAFARAEPLFADVAPEEqGYL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  160 YAGRVGSGHFLKMVHNGIEYGMMQAIAEGFEVLDKSDFDFNYEDVAKVWANGSVIRGWLMDLTEKAFADDPKLDGIKGVM 239
Cdd:TIGR00872 160 YCGPCGSGHFVKMVHNGIEYGMMAAIAEGFEILRNSQFDFDIPEVARVWRRGSVIRSWLLDLTAIAFRESPDLAEFSGRV 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446688635  240 NSSGEGKWTVETALELQAAAPVIAMSLFMRYRSQEDDTFHGKVVSALRNQFGGHEVVKK 298
Cdd:TIGR00872 240 SDSGEGRWTVIAAIDLGVPAPVIATSLQSRFASRDLDDFANKVLAALRKEFGGHAEKKK 298
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 2-153 7.75e-48

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: 157.25  E-value: 7.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635    2 KLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVEKAGKLGITARHTLKEMIAELeapRTIWVMVPAGEVVESVL--KD 79
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGL---DVVITMVPAGAAVDAVIfgEG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446688635   80 VYPLLDEGDIVIEGGNSFYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGAC-LMVGGEKEIYDQLEPLFKDLA 153
Cdd:pfam03446  78 LLPGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLsIMVGGDEEAFERVKPILEAMG 152
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
 7-42 2.80e-03

NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. Amino acid DH -like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133444  Cd Length: 200  Bit Score: 37.96  E-value: 2.80e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 446688635   7 GLGKMGFPLAEHLHEDKHEVVVYDVNKELVEKAGKL 42
Cdd:cd01075   35 GLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAEL 70
 
Name Accession Description Interval E-value
YqeC COG1023
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
1-298 0e+00

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


Pssm-ID: 440646 [Multi-domain]  Cd Length: 300  Bit Score: 545.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   1 MKLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVEKAGKLGITARHTLKEMIAELEAPRTIWVMVPAGEVVESVLKDV 80
Cdd:COG1023    1 MQIGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKLPAPRVVWLMVPAGEITDQVIEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  81 YPLLDEGDIVIEGGNSFYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGACLMVGGEKEIYDQLEPLFKDLAV--ENGY 158
Cdd:COG1023   81 APLLEPGDIVIDGGNSNYKDDIRRAEELAEKGIHFVDVGTSGGVWGLENGYCLMIGGDKEAVERLEPIFKALAPgaENGY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635 159 SYAGRVGSGHFLKMVHNGIEYGMMQAIAEGFEVLDKSDFDFNYEDVAKVWANGSVIRGWLMDLTEKAFADDPKLDGIKGV 238
Cdd:COG1023  161 LHCGPVGAGHFVKMVHNGIEYGMMQAYAEGFELLEASEFDLDLAEVAEVWRRGSVIRSWLLDLTADALAEDPKLEGISGY 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635 239 MNSSGEGKWTVETALELQAAAPVIAMSLFMRYRSQEDDTFHGKVVSALRNQFGGHEVVKK 298
Cdd:COG1023  241 VEDSGEGRWTVEEAIELGVPAPVITAALFARFRSRQEDSFADKVLAALRNQFGGHAVKKK 300
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
1-298 0e+00

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 530.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   1 MKLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVEKAGKLGITARHTLKEMIAELEAPRTIWVMVPAGEVVESVLKDV 80
Cdd:PRK09599   1 MQLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPAPRVVWLMVPAGEITDATIDEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  81 YPLLDEGDIVIEGGNSFYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGACLMVGGEKEIYDQLEPLFKDLAV--ENGY 158
Cdd:PRK09599  81 APLLSPGDIVIDGGNSYYKDDIRRAELLAEKGIHFVDVGTSGGVWGLERGYCLMIGGDKEAVERLEPIFKALAPraEDGY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635 159 SYAGRVGSGHFLKMVHNGIEYGMMQAIAEGFEVLDKSDFDFNYEDVAKVWANGSVIRGWLMDLTEKAFADDPKLDGIKGV 238
Cdd:PRK09599 161 LHAGPVGAGHFVKMVHNGIEYGMMQAYAEGFELLEASRFDLDLAAVAEVWRRGSVIRSWLLDLTADALAEDPKLDEISGY 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635 239 MNSSGEGKWTVETALELQAAAPVIAMSLFMRYRSQEDDTFHGKVVSALRNQFGGHEVVKK 298
Cdd:PRK09599 241 VEDSGEGRWTVEEAIDLAVPAPVIAAALFMRFRSRQEDSFADKVVAALRNGFGGHAVKKK 300
gnd_rel TIGR00872
6-phosphogluconate dehydrogenase (decarboxylating); This family resembles a larger family (gnd) ...
 1-298 6.07e-138

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: 391.52  E-value: 6.07e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635    1 MKLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVEKAGKLGITARHTLKEMIAELEAPRTIWVMVPAGeVVESVLKDV 80
Cdd:TIGR00872   1 MQLGLIGLGRMGANIVRRLAKRGHDCVGYDHDQDAVKAMKEDRTTGVANLRELSQRLSAPRVVWVMVPHG-IVDAVLEEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   81 YPLLDEGDIVIEGGNSFYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGACLMVGGEKEIYDQLEPLFKDLAVEN-GYS 159
Cdd:TIGR00872  80 APTLEKGDIVIDGGNSYYKDSLRRYKLLKEKGIHLLDCGTSGGVWGRERGYCFMIGGDGEAFARAEPLFADVAPEEqGYL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  160 YAGRVGSGHFLKMVHNGIEYGMMQAIAEGFEVLDKSDFDFNYEDVAKVWANGSVIRGWLMDLTEKAFADDPKLDGIKGVM 239
Cdd:TIGR00872 160 YCGPCGSGHFVKMVHNGIEYGMMAAIAEGFEILRNSQFDFDIPEVARVWRRGSVIRSWLLDLTAIAFRESPDLAEFSGRV 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446688635  240 NSSGEGKWTVETALELQAAAPVIAMSLFMRYRSQEDDTFHGKVVSALRNQFGGHEVVKK 298
Cdd:TIGR00872 240 SDSGEGRWTVIAAIDLGVPAPVIATSLQSRFASRDLDDFANKVLAALRKEFGGHAEKKK 298
Gnd COG0362
6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate ...
 4-272 4.70e-83

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: 257.69  E-value: 4.70e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   4 GLIGLGKMGFPLAEHLhEDK-HEVVVYD----VNKELVEKAGKLG-ITARHTLKEMIAELEAPRTIWVMVPAGEVVESVL 77
Cdd:COG0362    6 GVIGLAVMGRNLALNI-ADHgFSVAVYNrtaeKTDAFLAEHGKGKnIVGTYSLEEFVASLERPRKILLMVKAGKPVDAVI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  78 KDVYPLLDEGDIVIEGGNSFYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGACLMVGGEKEIYDQLEPLFKDLA--VE 155
Cdd:COG0362   85 EQLLPLLEPGDIIIDGGNSHFTDTIRREKELAEKGIHFIGMGVSGGEEGALHGPSIMPGGSKEAYELVKPILEAIAakVD 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635 156 NG--YSYAGRVGSGHFLKMVHNGIEYGMMQAIAEGFEVLdKSDFDFNYEDVAKVWA--NGSVIRGWLMDLTEKAFA-DDP 230
Cdd:COG0362  165 GEpcVTYIGPDGAGHFVKMVHNGIEYADMQLIAEAYDLL-RDGLGLSNDEIAEVFAewNKGELDSYLIEITADILRkKDP 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 446688635 231 K-----LDGIKGVMNSSGEGKWTVETALELQAAAPVIAMSLFMRYRS 272
Cdd:COG0362  244 EtgkplVDVILDKAGQKGTGKWTSQSALDLGVPLPLITEAVFARYLS 290
PRK09287 PRK09287
NADP-dependent phosphogluconate dehydrogenase;
11-272 7.15e-76

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236453 [Multi-domain]  Cd Length: 459  Bit Score: 238.87  E-value: 7.15e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  11 MGFPLAEHLHEDKHEVVVYDVNK----ELVEKAGKLG-ITARHTLKEMIAELEAPRTIWVMVPAGEVVESVLKDVYPLLD 85
Cdd:PRK09287   1 MGKNLALNIASHGYTVAVYNRTPektdEFLAEEGKGKkIVPAYTLEEFVASLEKPRKILLMVKAGAPVDAVIEQLLPLLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  86 EGDIVIEGGNSFYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGACLMVGGEKEIYDQLEPLFKDLA--VENGY---SY 160
Cdd:PRK09287  81 KGDIIIDGGNSNYKDTIRREKELAEKGIHFIGMGVSGGEEGALHGPSIMPGGQKEAYELVAPILEKIAakVEDGEpcvTY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635 161 AGRVGSGHFLKMVHNGIEYGMMQAIAEGFEVLdKSDFDFNYEDVAKV---WANGSViRGWLMDLTEKAFA------DDPK 231
Cdd:PRK09287 161 IGPDGAGHYVKMVHNGIEYGDMQLIAEAYDLL-KDGLGLSAEEIADVfaeWNKGEL-NSYLIEITADILRqkdeetGKPL 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 446688635 232 LDGIKGVMNSSGEGKWTVETALELQAAAPVIAMSLFMRYRS 272
Cdd:PRK09287 239 VDVILDKAGQKGTGKWTSQSALDLGVPLTLITEAVFARYLS 279
gnd TIGR00873
6-phosphogluconate dehydrogenase (decarboxylating); This model does not specify whether the ...
 3-272 1.12e-70

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: 225.74  E-value: 1.12e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635    3 LGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVEK------AGKlGITARHTLKEMIAELEAPRTIWVMVPAGEVVESV 76
Cdd:TIGR00873   2 IGVIGLAVMGQNLALNMEDHGFTVSVYNRTPSKTDEflaeeaKGK-SIIGAYSIEDFVQSLERPRKIMLMVKAGAPVDAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   77 LKDVYPLLDEGDIVIEGGNSFYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGACLMVGGEKEIYDQLEPLFKDLAVEN 156
Cdd:TIGR00873  81 IDSLLPLLEKGDIIIDGGNSHYPDTERRYKELKAKGILFVGSGVSGGEEGARKGPSIMPGGSPEAWPLVAPIFQSIAAKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  157 G----YSYAGRVGSGHFLKMVHNGIEYGMMQAIAEGFEVLdKSDFDFNYEDVAKV---WANGsVIRGWLMDLTEKAFA-D 228
Cdd:TIGR00873 161 DgepcCTWVGPGGAGHYVKMVHNGIEYGDMQLICEAYDIL-KRGLGLSNEEIAEIfteWNNG-ELDSYLIEITADILAkK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 446688635  229 DPK----LDGIKGVMNSSGEGKWTVETALELQAAAPVIAMSLFMRYRS 272
Cdd:TIGR00873 239 DEDgnplVDKILDTAGQKGTGKWTAINALDLGVPLTLITESVFARYLS 286
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 3-272 4.42e-68

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 219.27  E-value: 4.42e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   3 LGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVE------KAGKLGITARHTLKEMIAELEAPRTIWVMVPAGEVVESV 76
Cdd:PTZ00142   4 IGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEefvkkaKEGNTRVKGYHTLEELVNSLKKPRKVILLIKAGEAVDET 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  77 LKDVYPLLDEGDIVIEGGNSFYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGACLMVGGEKEIYDQLEPLFKDLAVEN 156
Cdd:PTZ00142  84 IDNLLPLLEKGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGPSLMPGGNKEAYDHVKDILEKCSAKV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635 157 GYS----YAGRVGSGHFLKMVHNGIEYGMMQAIAEGFEVLdKSDFDFNYEDVAKVWA--NGSVIRGWLMDLTEKAFA--- 227
Cdd:PTZ00142 164 GDSpcvtYVGPGSSGHYVKMVHNGIEYGDMQLISESYKLM-KHILGMSNEELSEVFNkwNEGILNSYLIEITAKILAkkd 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 446688635 228 ---DDPKLDGIKGVMNSSGEGKWTVETALELQAAAPVIAMSLFMRYRS 272
Cdd:PTZ00142 243 dlgEEHLVDKILDIAGSKGTGKWTVQEALERGIPVPTMAASVDARNIS 290
PLN02350 PLN02350
phosphogluconate dehydrogenase (decarboxylating)
 2-272 8.31e-62

phosphogluconate dehydrogenase (decarboxylating)


Pssm-ID: 215200 [Multi-domain]  Cd Length: 493  Bit Score: 203.41  E-value: 8.31e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   2 KLGLIGLGKMGFPLAEHLHEDKHEVVVY----DVNKELVEKA---GKLGITARHTLKEMIAELEAPRTIWVMVPAGEVVE 74
Cdd:PLN02350   8 RIGLAGLAVMGQNLALNIAEKGFPISVYnrttSKVDETVERAkkeGNLPLYGFKDPEDFVLSIQKPRSVIILVKAGAPVD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  75 SVLKDVYPLLDEGDIVIEGGNSFYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGACLMVGGEKEIYDQLEPLFKDLA- 153
Cdd:PLN02350  88 QTIKALSEYMEPGDCIIDGGNEWYENTERRIKEAAEKGLLYLGMGVSGGEEGARNGPSLMPGGSFEAYKNIEDILEKVAa 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635 154 -VENG--YSYAGRVGSGHFLKMVHNGIEYGMMQAIAEGFEVLdKSDFDFNYEDVAKVWA--NGSVIRGWLMDLTEKAFA- 227
Cdd:PLN02350 168 qVDDGpcVTYIGPGGAGNFVKMVHNGIEYGDMQLISEAYDVL-KSVGGLSNEELAEVFAewNKGELESFLIEITADIFSv 246

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 446688635 228 -----DDPKLDGIKGVMNSSGEGKWTVETALELQAAAPVIAMSLFMRYRS 272
Cdd:PLN02350 247 kddkgDGYLVDKILDKTGMKGTGKWTVQQAAELSVAAPTIAASLDARYLS 296
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 2-153 7.75e-48

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: 157.25  E-value: 7.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635    2 KLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVEKAGKLGITARHTLKEMIAELeapRTIWVMVPAGEVVESVL--KD 79
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGL---DVVITMVPAGAAVDAVIfgEG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446688635   80 VYPLLDEGDIVIEGGNSFYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGAC-LMVGGEKEIYDQLEPLFKDLA 153
Cdd:pfam03446  78 LLPGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLsIMVGGDEEAFERVKPILEAMG 152
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-220 2.27e-38

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 136.78  E-value: 2.27e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   1 MKLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVEKAGKLGITARHTLKEMIAELEAprtIWVMVPAGEVVESVL--- 77
Cdd:COG2084    2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADV---VITMLPDDAAVEEVLlge 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  78 KDVYPLLDEGDIVIEGGNSFYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGAC-LMVGGEKEIYDQLEPLFKDLAveN 156
Cdd:COG2084   79 DGLLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLtIMVGGDEAAFERARPVLEAMG--K 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446688635 157 GYSYAGRVGSGHFLKMVHNGIEYGMMQAIAEGFEVLDKSDFDFnyEDVAKVWANGSViRGWLMD 220
Cdd:COG2084  157 RIVHVGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDP--ETLLEVLSGGAA-GSWVLE 217
6PGD pfam00393
6-phosphogluconate dehydrogenase, C-terminal domain; This family represents the C-terminal ...
 167-272 5.33e-28

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: 109.47  E-value: 5.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  167 GHFLKMVHNGIEYGMMQAIAEGFEVLdKSDFDFNYEDVAKVWA--NGSVIRGWLMDLTEKAFA-DDPK-----LDGIKGV 238
Cdd:pfam00393   1 GHYVKMVHNGIEYGDMQLIAEAYDLL-KRGLGLSNDEIADVFEewNKGELDSYLIEITADILRkKDPEdgkplVDKILDK 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 446688635  239 MNSSGEGKWTVETALELQAAAPVIAMSLFMRYRS 272
Cdd:pfam00393  80 AGQKGTGKWTVQEALDLGVPAPTIAEAVFARCLS 113
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-189 5.77e-20

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 87.80  E-value: 5.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   1 MKLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVEKAGKLGITARHTLKEMIAELEaprTIWVMVPAGEVVESVLKDV 80
Cdd:PRK11559   3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCD---VIITMLPNSPHVKEVALGE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  81 YPLLD---EGDIVIEGGNSFYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGA-CLMVGGEKEIYDQLEPLFKDLAVEn 156
Cdd:PRK11559  80 NGIIEgakPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTlSVMVGGDKAIFDKYYDLMKAMAGS- 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446688635 157 gYSYAGRVGSGHFLKMVHNGIEYGMMQAIAEGF 189
Cdd:PRK11559 159 -VVHTGDIGAGNVTKLANQVIVALNIAAMSEAL 190
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
1-198 1.78e-15

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 75.06  E-value: 1.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   1 MKLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKeLVEKAGKLGITARHTLKEMIaelEAPRTIWVMVPAGEVVESVL--- 77
Cdd:PRK15059   1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGP-VADELLSLGAVSVETARQVT---EASDIIFIMVPDTPQVEEVLfge 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  78 KDVYPLLDEGDIVIEGGNSFYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGA-CLMVGGEKEIYDQLEPLFKDLAveN 156
Cdd:PRK15059  77 NGCTKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTlSIMVGGDEAVFERVKPLFELLG--K 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446688635 157 GYSYAGRVGSGHFLKMVHNGIEYGMMQAIAEGFEVLDKSDFD 198
Cdd:PRK15059 155 NITLVGGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGAD 196
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
2-175 6.34e-11

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 61.80  E-value: 6.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   2 KLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKE----LVEKAGKLGITARHTLKEmiAELeaprtIWVMVPAGEVVESVL 77
Cdd:PRK15461   3 AIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQavdaLVDKGATPAASPAQAAAG--AEF-----VITMLPNGDLVRSVL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  78 ---KDVYPLLDEGDIVIEGG--NSFYKDTLRRAEEAKSFGLHYVDIGTSgGVEGARYGACLMVGGEKEIYDQLEPLFkdL 152
Cdd:PRK15461  76 fgeNGVCEGLSRDALVIDMStiHPLQTDKLIADMQAKGFSMMDVPVGRT-SDNAITGTLLLLAGGTAEQVERATPIL--M 152

                        170       180
                 ....*....|....*....|...
gi 446688635 153 AVENGYSYAGRVGSGHFLKMVHN 175
Cdd:PRK15461 153 AMGNELINAGGPGMGIRVKLINN 175
PLN02858 PLN02858
fructose-bisphosphate aldolase
 2-174 3.23e-10

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 61.02  E-value: 3.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635    2 KLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVEKAGKLGITARHTLKEMIAELEaprTIWVMVPAGEVVESVL---- 77
Cdd:PLN02858  326 RIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVD---VLVIMVANEVQAENVLfgdl 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   78 KDVYPLLDEGDIVIEGGNS-FYKDTLRRAEEAKSFGLHYVDIGTSGGVEGARYGA-CLMVGGEKEIYDQLEPLFKDLAvE 155
Cdd:PLN02858  403 GAVSALPAGASIVLSSTVSpGFVIQLERRLENEGRDIKLVDAPVSGGVKRAAMGTlTIMASGTDEALKSAGSVLSALS-E 481

                         170
                  ....*....|....*....
gi 446688635  156 NGYSYAGRVGSGHFLKMVH 174
Cdd:PLN02858  482 KLYVIKGGCGAGSGVKMVN 500
6PGD pfam00393
6-phosphogluconate dehydrogenase, C-terminal domain; This family represents the C-terminal ...
 169-293 1.74e-08

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: 54.38  E-value: 1.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635  169 FLKMVHNGIEYGMMQAIAEGFEVLDKS----DFDFNYEDVAKVWANGSVIRGWLMDLTEKAFADDPKL------DGIKGV 238
Cdd:pfam00393 141 FIEDLRQALYASKIISYAQGFALLRAAskeyGWNLNLGEIARIWRGGCIIRADFLDKIKEAYKKNPDLsnllldPYFAKE 220

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446688635  239 MNSSGEG-KWTVETALELQAAAPVIAMSL--FMRYRSqedDTFHGKVVSALRNQFGGH 293
Cdd:pfam00393 221 LKEAQPSwRRVVALAVEAGIPVPALSAALsyYDGYRS---ERLPANLIQAQRDYFGAH 275
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 1-48 6.69e-06

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 46.60  E-value: 6.69e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446688635   1 MKLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVEKAGKLGITARH 48
Cdd:COG0569   96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIV 143
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-91 1.39e-05

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 45.44  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   1 MKLGLIGLGKMGFPLAEHLHE---DKHEVVVYDVNKELVEK-AGKLGITARHTLKEMIAelEAPRTIWVMVPAgeVVESV 76
Cdd:COG0345    3 MKIGFIGAGNMGSAIIKGLLKsgvPPEDIIVSDRSPERLEAlAERYGVRVTTDNAEAAA--QADVVVLAVKPQ--DLAEV 78

                         90
                 ....*....|....*
gi 446688635  77 LKDVYPLLDEGDIVI 91
Cdd:COG0345   79 LEELAPLLDPDKLVI 93
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
2-91 1.68e-05

UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 45.82  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   2 KLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVE--KAGKLGI--TARHTLKEMIAE-----------LEAPRTIWVM 66
Cdd:COG0677    1 KIAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEelNAGEDPIlePGDELLAEAVAAgrlrattdpeaLAEADVVIIA 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446688635  67 VP-----AGEV----VESVLKDVYPLLDEGDIVI 91
Cdd:COG0677   81 VPtpldeDKEPdlsyLESASETIAPHLKPGDLVV 114
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 1-91 5.26e-05

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 44.14  E-value: 5.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635    1 MKLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVEK--AGKLGItARHTLKEMIAE-LEAPR---------------T 62
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKlnKGKSPI-YEPGLDELLAKaLKAGRlrattdyeeairdadV 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 446688635   63 IWVMVPA-----GEV----VESVLKDVYPLLDEGDIVI 91
Cdd:TIGR03026  80 IIICVPTplkedGSPdlsyVESAAETIAKHLRKGATVV 117
trkA PRK09496
Trk system potassium transporter TrkA;
1-39 4.50e-04

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 41.65  E-value: 4.50e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 446688635   1 MKLGLIGLGKMGFPLAEHLHEDKHEVVVYDVNKELVEKA 39
Cdd:PRK09496   1 MKIIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRL 39
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 1-91 6.42e-04

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 41.13  E-value: 6.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   1 MKLGLIG-LGKMGFPLAEHLHEDKHEVVVYDVN-KELVEKAGKLGITARHTLKEMIAELEaprTIWVMVPAgEVVESVLK 78
Cdd:PRK08655   1 MKISIIGgTGGLGKWFARFLKEKGFEVIVTGRDpKKGKEVAKELGVEYANDNIDAAKDAD---IVIISVPI-NVTEDVIK 76

                         90
                 ....*....|...
gi 446688635  79 DVYPLLDEGDIVI 91
Cdd:PRK08655  77 EVAPHVKEGSLLM 89
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 1-94 1.12e-03

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 39.72  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   1 MKLGLIGLGKMG--FPLAEHLHEDKHEVVVYDVNKELVEKAGKLGITAR--HTLKEMI--AELeaprtIWVMVPAGEVVE 74
Cdd:COG0287    2 MRIAIIGLGLIGgsLALALKRAGLAHEVVGVDRSPETLERALELGVIDRaaTDLEEAVadADL-----VVLAVPVGATIE 76

                         90       100
                 ....*....|....*....|
gi 446688635  75 sVLKDVYPLLDEGDIVIEGG 94
Cdd:COG0287   77 -VLAELAPHLKPGAIVTDVG 95
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-58 1.32e-03

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 39.52  E-value: 1.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446688635   1 MKLGLIGLGKMGFPLAEHLHEDKH-EVV-VYDVNKELVEK-AGKLGITARHTLKEMIAELE 58
Cdd:COG0673    4 LRVGIIGAGGIGRAHAPALAALPGvELVaVADRDPERAEAfAEEYGVRVYTDYEELLADPD 64
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-56 1.68e-03

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 39.41  E-value: 1.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446688635   1 MKLGLIGLGKMGFPLAEHLHEDKHEVV-VYDVNKELVEK-AGKLGITARHTLKEMIAE 56
Cdd:COG5495    4 MKIGIIGAGRVGTALAAALRAAGHEVVgVYSRSPASAERaAALLGAVPALDLEELAAE 61
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
 7-42 2.80e-03

NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. Amino acid DH -like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133444  Cd Length: 200  Bit Score: 37.96  E-value: 2.80e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 446688635   7 GLGKMGFPLAEHLHEDKHEVVVYDVNKELVEKAGKL 42
Cdd:cd01075   35 GLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAEL 70
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 5-67 3.29e-03

TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.


Pssm-ID: 426679 [Multi-domain]  Cd Length: 115  Bit Score: 36.73  E-value: 3.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446688635    5 LIGLGKMGFPLAEHLHEDkHEVVVYDVNKELVEKAGKLGITARH---TLKEMIAELEAPRTIWVMV 67
Cdd:pfam02254   3 IIGYGRVGRSLAEELSEG-GDVVVIDKDEERVEELREEGVPVVVgdaTDEEVLEEAGIEEADAVIA 67
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
 2-94 3.40e-03

bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 38.82  E-value: 3.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446688635   2 KLGLIGLGKMGFPLAEHLHEDK--HEVVVYDVNKELVEKAGKLGITARHTlkEMIAE-LEAPRTIWVMVPAGeVVESVLK 78
Cdd:PRK14806   5 RVVVIGLGLIGGSFAKALRERGlaREVVAVDRRAKSLELAVSLGVIDRGE--EDLAEaVSGADVIVLAVPVL-AMEKVLA 81

                         90
                 ....*....|....*.
gi 446688635  79 DVYPLLDEGDIVIEGG 94
Cdd:PRK14806  82 DLKPLLSEHAIVTDVG 97
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 1-59 6.41e-03

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 36.75  E-value: 6.41e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446688635   1 MKLGLIGLGKMGFPLAEHLHEDK-HEVV-VYDVNKELVEK-------AGKLGITARHTLKEMIAELEA 59
Cdd:cd24146    1 IRVVVWGLGAMGRGIARYLLEKPgLEIVgAVDRDPAKVGKdlgelggGAPLGVKVTDDLDAVLAATKP 68
 
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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