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Conserved domains on  [gi|488044815|ref|WP_002116212|]
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MULTISPECIES: NAD(P)-dependent oxidoreductase [Acinetobacter]

Protein Classification

NAD(P)-dependent oxidoreductase( domain architecture ID 11449905)

NAD(P)-dependent oxidoreductase similar to 3-hydroxyisobutyrate dehydrogenase, L-threonate dehydrogenase, 2-(hydroxymethyl)glutarate dehydrogenase, and glyoxylate/succinic semialdehyde reductase

CATH:  3.40.50.720
EC:  1.1.-.-
Gene Ontology:  GO:0050661|GO:0051287|GO:0016491
PubMed:  8749365
SCOP:  4000072

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 5-281 6.02e-91

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


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 271.22  E-value: 6.02e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   5 VSFIGLGAMGWHMASHLTQVCSQVYVWNRTFAKAKQHEQTFGTQAVDLTQAL-QADIIFSCLPTSQDVENLIAD-----S 78
Cdd:COG2084    4 VGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAaAADVVITMLPDDAAVEEVLLGedgllA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815  79 QLKQGCIWVDCTSGVPETARKLSQQLKVNGVDYLDAPVSGQTIGAERGTLTVMVGGDESAFKRAKPIIQAFANLVEYVGE 158
Cdd:COG2084   84 ALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVGD 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815 159 SGAAFAVKAINNTLMATHLWALAEGLSILKSQGVNLHSAMNCINHSSGKSNVSEHiMMQRILNRKFEKTFALDLLQKDIG 238
Cdd:COG2084  164 AGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLEN-RGPRMLAGDFDPGFALDLMLKDLG 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 488044815 239 IALNLVTQNNLELPAFSLIQQQFNQVSKPDAQQVDFSAIVKLL 281
Cdd:COG2084  243 LALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 5-281 6.02e-91

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 271.22  E-value: 6.02e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   5 VSFIGLGAMGWHMASHLTQVCSQVYVWNRTFAKAKQHEQTFGTQAVDLTQAL-QADIIFSCLPTSQDVENLIAD-----S 78
Cdd:COG2084    4 VGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAaAADVVITMLPDDAAVEEVLLGedgllA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815  79 QLKQGCIWVDCTSGVPETARKLSQQLKVNGVDYLDAPVSGQTIGAERGTLTVMVGGDESAFKRAKPIIQAFANLVEYVGE 158
Cdd:COG2084   84 ALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVGD 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815 159 SGAAFAVKAINNTLMATHLWALAEGLSILKSQGVNLHSAMNCINHSSGKSNVSEHiMMQRILNRKFEKTFALDLLQKDIG 238
Cdd:COG2084  164 AGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLEN-RGPRMLAGDFDPGFALDLMLKDLG 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 488044815 239 IALNLVTQNNLELPAFSLIQQQFNQVSKPDAQQVDFSAIVKLL 281
Cdd:COG2084  243 LALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 5-289 4.43e-50

2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60), also called tartronate semialdehyde reductase. It follows glyoxylate carboligase and precedes glycerate kinase in D-glycerate pathway of glyoxylate degradation. The eventual product, 3-phosphoglycerate, is an intermediate of glycolysis and is readily metabolized. Tartronic semialdehyde, the substrate of this enzyme, may also come from other pathways, such as D-glucarate catabolism.


Pssm-ID: 130569 [Multi-domain]  Cd Length: 291  Bit Score: 166.99  E-value: 4.43e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815    5 VSFIGLGAMGWHMASHLTQVCSQVYVWNRTFAKAKQHEQTFGTQAVDLTQAL-QADIIFSCLPTSQDVE------NLIAD 77
Cdd:TIGR01505   2 VGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTeQADVIFTMVPDSPQVEevafgeNGIIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   78 SQlKQGCIWVDCTSGVPETARKLSQQLKVNGVDYLDAPVSGQTIGAERGTLTVMVGGDESAFKRAKPIIQAFANLVEYVG 157
Cdd:TIGR01505  82 GA-KPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815  158 ESGAAFAVKAINNTLMATHLWALAEGLSILKSQGVNLHSAMNCINHSSGKSNVSEhIMMQRILNRKFEKTFALDLLQKDI 237
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLE-VKGERVIDRTFKPGFRIDLHQKDL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 488044815  238 GIALNLVTQNNLELPAFSLIQQQFNQVSKPDAQQVDFSAIVKLLEQQNQLEL 289
Cdd:TIGR01505 240 NLALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALELLANHKV 291
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 4-157 2.64e-49

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: 160.71  E-value: 2.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815    4 SVSFIGLGAMGWHMASHLTQVCSQVYVWNRTFAKAKQHEQTFGTQAVDLTQALQ-ADIIFSCLPTSQDVENLIADSQ--- 79
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAgLDVVITMVPAGAAVDAVIFGEGllp 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488044815   80 -LKQGCIWVDCTSGVPETARKLSQQLKVNGVDYLDAPVSGQTIGAERGTLTVMVGGDESAFKRAKPIIQAFANLVEYVG 157
Cdd:pfam03446  81 gLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-283 9.22e-41

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 142.88  E-value: 9.22e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   1 MIQSVSFIGLGAMGWHMASHLTQVCSQVYVWNRT---FAKAKQHEQTFGTQAVDLtqALQADIIFSCLPTSQDV------ 71
Cdd:PRK11559   1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNpeaVAEVIAAGAETASTAKAV--AEQCDVIITMLPNSPHVkevalg 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815  72 ENLIADSqLKQGCIWVDCTSGVPETARKLSQQLKVNGVDYLDAPVSGQTIGAERGTLTVMVGGDESAFKRAKPIIQAFAN 151
Cdd:PRK11559  79 ENGIIEG-AKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815 152 LVEYVGESGAAFAVKAINNTLMATHLWALAEGLSILKSQGVNLHSAMNCINHSSGKSNVSEHiMMQRILNRKFEKTFALD 231
Cdd:PRK11559 158 SVVHTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDA-KAPMVMDRNFKPGFRID 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488044815 232 LLQKDIGIALNLVTQNNLELPAFSLIQQQFNQVSKPDAQQVDFSAIVKLLEQ 283
Cdd:PRK11559 237 LHIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEK 288
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 5-64 1.46e-04

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (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: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 42.64  E-value: 1.46e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488044815   5 VSFIGLGAMGWHMASHLTQV-CSQVYVWNRTFAKAKQHEQTFGTQAVDLTQAL----QADIIFSC 64
Cdd:cd05213  181 VLVIGAGEMGELAAKHLAAKgVAEITIANRTYERAEELAKELGGNAVPLDELLellnEADVVISA 245
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 5-281 6.02e-91

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 271.22  E-value: 6.02e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   5 VSFIGLGAMGWHMASHLTQVCSQVYVWNRTFAKAKQHEQTFGTQAVDLTQAL-QADIIFSCLPTSQDVENLIAD-----S 78
Cdd:COG2084    4 VGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAaAADVVITMLPDDAAVEEVLLGedgllA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815  79 QLKQGCIWVDCTSGVPETARKLSQQLKVNGVDYLDAPVSGQTIGAERGTLTVMVGGDESAFKRAKPIIQAFANLVEYVGE 158
Cdd:COG2084   84 ALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVGD 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815 159 SGAAFAVKAINNTLMATHLWALAEGLSILKSQGVNLHSAMNCINHSSGKSNVSEHiMMQRILNRKFEKTFALDLLQKDIG 238
Cdd:COG2084  164 AGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLEN-RGPRMLAGDFDPGFALDLMLKDLG 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 488044815 239 IALNLVTQNNLELPAFSLIQQQFNQVSKPDAQQVDFSAIVKLL 281
Cdd:COG2084  243 LALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 5-289 4.43e-50

2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60), also called tartronate semialdehyde reductase. It follows glyoxylate carboligase and precedes glycerate kinase in D-glycerate pathway of glyoxylate degradation. The eventual product, 3-phosphoglycerate, is an intermediate of glycolysis and is readily metabolized. Tartronic semialdehyde, the substrate of this enzyme, may also come from other pathways, such as D-glucarate catabolism.


Pssm-ID: 130569 [Multi-domain]  Cd Length: 291  Bit Score: 166.99  E-value: 4.43e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815    5 VSFIGLGAMGWHMASHLTQVCSQVYVWNRTFAKAKQHEQTFGTQAVDLTQAL-QADIIFSCLPTSQDVE------NLIAD 77
Cdd:TIGR01505   2 VGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTeQADVIFTMVPDSPQVEevafgeNGIIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   78 SQlKQGCIWVDCTSGVPETARKLSQQLKVNGVDYLDAPVSGQTIGAERGTLTVMVGGDESAFKRAKPIIQAFANLVEYVG 157
Cdd:TIGR01505  82 GA-KPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815  158 ESGAAFAVKAINNTLMATHLWALAEGLSILKSQGVNLHSAMNCINHSSGKSNVSEhIMMQRILNRKFEKTFALDLLQKDI 237
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLE-VKGERVIDRTFKPGFRIDLHQKDL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 488044815  238 GIALNLVTQNNLELPAFSLIQQQFNQVSKPDAQQVDFSAIVKLLEQQNQLEL 289
Cdd:TIGR01505 240 NLALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALELLANHKV 291
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 4-157 2.64e-49

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: 160.71  E-value: 2.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815    4 SVSFIGLGAMGWHMASHLTQVCSQVYVWNRTFAKAKQHEQTFGTQAVDLTQALQ-ADIIFSCLPTSQDVENLIADSQ--- 79
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAgLDVVITMVPAGAAVDAVIFGEGllp 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488044815   80 -LKQGCIWVDCTSGVPETARKLSQQLKVNGVDYLDAPVSGQTIGAERGTLTVMVGGDESAFKRAKPIIQAFANLVEYVG 157
Cdd:pfam03446  81 gLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 7-281 1.15e-43

3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that catalyzes the NAD+-dependent oxidation of 3-hydroxyisobutyrate to methylmalonate semialdehyde of the valine catabolism pathway. In Pseudomonas aeruginosa, 3-hydroxyisobutyrate dehydrogenase (mmsB) is co-induced with methylmalonate-semialdehyde dehydrogenase (mmsA) when grown on medium containing valine as the sole carbon source. The positive transcriptional regulator of this operon (mmsR) is located upstream of these genes and has been identified as a member of the XylS/AraC family of transcriptional regulators. 3-hydroxyisobutyrate dehydrogenase shares high sequence homology to the characterized 3-hydroxyisobutyrate dehydrogenase from rat liver with conservation of proposed NAD+ binding residues at the N-terminus (G-8,10,13,24 and D-31). This enzyme belongs to the 3-hydroxyacid dehydrogenase family, sharing a common evolutionary origin and enzymatic mechanism with 6-phosphogluconate. HIBADH exhibits sequence similarity to the NAD binding domain of 6-phosphogluconate dehydrogenase above trusted (pfam03446). [Energy metabolism, Amino acids and amines]


Pssm-ID: 130753 [Multi-domain]  Cd Length: 288  Bit Score: 150.33  E-value: 1.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815    7 FIGLGAMGWHMASHLTQVCSQVYVWNrTFAKAKQHEQTFGTQAVD--LTQALQADIIFSCLPTSQDVENLIADSQ----- 79
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFD-LFPDAVEEAVAAGAQAAAspAEAAEGADRVITMLPAGQHVISVYSGDEgilpk 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   80 LKQGCIWVDCTSGVPETARKLSQQLKVNGVDYLDAPVSGQTIGAERGTLTVMVGGDESAFKRAKPIIQAFANLVEYVGES 159
Cdd:TIGR01692  80 VAKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815  160 GAAFAVKAINNTLMATHLWALAEGLSILKSQGVNLHSAMNCINHSSGKS------NVSEHIMMQRILNRKFEKTFALDLL 233
Cdd:TIGR01692 160 GAGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCwssdtyNPVPGVMPQAPASNGYQGGFGTALM 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 488044815  234 QKDIGIALNLVTQNNLELPAFSLIQQQFNQVSKPDAQQVDFSAIVKLL 281
Cdd:TIGR01692 240 LKDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-283 9.22e-41

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 142.88  E-value: 9.22e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   1 MIQSVSFIGLGAMGWHMASHLTQVCSQVYVWNRT---FAKAKQHEQTFGTQAVDLtqALQADIIFSCLPTSQDV------ 71
Cdd:PRK11559   1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNpeaVAEVIAAGAETASTAKAV--AEQCDVIITMLPNSPHVkevalg 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815  72 ENLIADSqLKQGCIWVDCTSGVPETARKLSQQLKVNGVDYLDAPVSGQTIGAERGTLTVMVGGDESAFKRAKPIIQAFAN 151
Cdd:PRK11559  79 ENGIIEG-AKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815 152 LVEYVGESGAAFAVKAINNTLMATHLWALAEGLSILKSQGVNLHSAMNCINHSSGKSNVSEHiMMQRILNRKFEKTFALD 231
Cdd:PRK11559 158 SVVHTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDA-KAPMVMDRNFKPGFRID 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488044815 232 LLQKDIGIALNLVTQNNLELPAFSLIQQQFNQVSKPDAQQVDFSAIVKLLEQ 283
Cdd:PRK11559 237 LHIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEK 288
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
5-282 1.21e-40

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 142.47  E-value: 1.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   5 VSFIGLGAMGWHMASHLTQVCSQVYVwnRTFAKAKQHEQTFGTQAVDLTQAL--QADIIFSCLPTSQDVENLI------A 76
Cdd:PRK15059   3 LGFIGLGIMGTPMAINLARAGHQLHV--TTIGPVADELLSLGAVSVETARQVteASDIIFIMVPDTPQVEEVLfgengcT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815  77 DSQLKqGCIWVDCTSGVPETARKLSQQLKVNGVDYLDAPVSGQTIGAERGTLTVMVGGDESAFKRAKPIIQAFANLVEYV 156
Cdd:PRK15059  81 KASLK-GKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815 157 GESGAAFAVKAINNTLMATHLWALAEGLSILKSQGVNLHSAMNCINHSSGKSNVSEhIMMQRILNRKFEKTFALDLLQKD 236
Cdd:PRK15059 160 GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILE-VHGERMIKRTFNPGFKIALHQKD 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 488044815 237 IGIALNLVTQNNLELPAFSLIQQQFNQVSKPDAQQVDFSAIVKLLE 282
Cdd:PRK15059 239 LNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALE 284
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 160-281 1.05e-36

NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidized to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure.


Pssm-ID: 434252 [Multi-domain]  Cd Length: 122  Bit Score: 126.87  E-value: 1.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815  160 GAAFAVKAINNTLMATHLWALAEGLSILKSQGVNLHSAMNCINHSSGKSNVSEHIMMQRILNRKFEKTFALDLLQKDIGI 239
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFPQRVLSRDFDPGFALDLMLKDLGL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 488044815  240 ALNLVTQNNLELPAFSLIQQQFNQVSKPDAQQVDFSAIVKLL 281
Cdd:pfam14833  81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
5-287 1.20e-26

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 105.71  E-value: 1.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   5 VSFIGLGAMGWHMASHLTQVCSQVYVWNRTfAKAKQHEQTFGTQAVDLTQ--ALQADIIFSCLPTSQDVENLIADSQ--- 79
Cdd:PRK15461   4 IAFIGLGQMGSPMASNLLKQGHQLQVFDVN-PQAVDALVDKGATPAASPAqaAAGAEFVITMLPNGDLVRSVLFGENgvc 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815  80 --LKQGCIWVDCTSGVPETARKLSQQLKVNGVDYLDAPVSGQTIGAERGTLTVMVGGDESAFKRAKPIIQAFANLVEYVG 157
Cdd:PRK15461  83 egLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815 158 ESGAAFAVKAINNtLMATHLWAL-AEGLSILKSQGVNLHSAMNCINHS-SGKSNVSEHiMMQRILNRKFEKTFALDLLQK 235
Cdd:PRK15461 163 GPGMGIRVKLINN-YMSIALNALsAEAAVLCEALGLSFDVALKVMSGTaAGKGHFTTT-WPNKVLKGDLSPAFMIDLAHK 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488044815 236 DIGIALNLVTQNNLELPAFSLIQQQFNQVSKPDAQQVDFSAIVKLLEQQNQL 287
Cdd:PRK15461 241 DLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSAGL 292
PLN02858 PLN02858
fructose-bisphosphate aldolase
 2-283 4.99e-25

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 104.93  E-value: 4.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815    2 IQSVSFIGLGAMGWHMASHLTQ----VCSqVYVWNRTFAKAKQHEQTFGTQAVDLTQalQADIIFSCLPTSQDVENLI-- 75
Cdd:PLN02858  324 VKRIGFIGLGAMGFGMASHLLKsnfsVCG-YDVYKPTLVRFENAGGLAGNSPAEVAK--DVDVLVIMVANEVQAENVLfg 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   76 ---ADSQLKQGCIWVDCTSGVPETARKLSQQLKVNGVD--YLDAPVSGQTIGAERGTLTVMVGGDESAFKRAKPIIQAFA 150
Cdd:PLN02858  401 dlgAVSALPAGASIVLSSTVSPGFVIQLERRLENEGRDikLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALS 480

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815  151 NLVEYV-GESGAAFAVKAINNTLMATHLWALAEGLSILKSQGVNLHSAMNCINHSSGKSNVSEHiMMQRILNRKFEKTFA 229
Cdd:PLN02858  481 EKLYVIkGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFEN-RVPHMLDNDYTPYSA 559

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488044815  230 LDLLQKDIGIALNLVTQNNLELPAFSLIQQQFNQVSKPDAQQVDFSAIVKLLEQ 283
Cdd:PLN02858  560 LDIFVKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVYET 613
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
7-194 2.61e-21

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 91.35  E-value: 2.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   7 FIGLGAMGWHMASHLTQVCSQVYVWNRTFAKAKQHEQTFGTQA---VDLTQALQAD-IIFSCLPTSQDVENLIAD--SQL 80
Cdd:PRK09599   5 MIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGAdslEELVAKLPAPrVVWLMVPAGEITDATIDElaPLL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815  81 KQGCIWVDC-TSGVPETARKlSQQLKVNGVDYLDAPVSGQTIGAERGTLTvMVGGDESAFKRAKPIIQAFANLVE----Y 155
Cdd:PRK09599  85 SPGDIVIDGgNSYYKDDIRR-AELLAEKGIHFVDVGTSGGVWGLERGYCL-MIGGDKEAVERLEPIFKALAPRAEdgylH 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 488044815 156 VGESGAAFAVKAINN----TLMAthlwALAEGLSILKSQGVNL 194
Cdd:PRK09599 163 AGPVGAGHFVKMVHNgieyGMMQ----AYAEGFELLEASRFDL 201
PLN02858 PLN02858
fructose-bisphosphate aldolase
 5-283 3.73e-19

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 87.60  E-value: 3.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815    5 VSFIGLGAMGWHMASHLTQVCSQVyvwnRTFAKAKQHEQTF----GTQAVDLTQALQADIIFSCLPTSQD-VENLIADSQ 79
Cdd:PLN02858    7 VGFVGLDSLSFELASSLLRSGFKV----QAFEISTPLMEKFcelgGHRCDSPAEAAKDAAALVVVLSHPDqVDDVFFGDE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   80 -----LKQGCIWVDCTSGVPETARKLSQQLKVNGVD--YLDAPVSGQTIGAERGTLTVMVGGDESAFKRAKPIIQAFANL 152
Cdd:PLN02858   83 gaakgLQKGAVILIRSTILPLQLQKLEKKLTERKEQifLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815  153 VEYV-GESGAAFAVKAINNTLMATHLWALAEGLSILKSQGVNLHSAMNCINHSSGKSNVSEHIMMQRILNRKFEKTFaLD 231
Cdd:PLN02858  163 LYTFeGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRF-LN 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 488044815  232 LLQKDIGIALNLVTQNNLELPAFSLIQQQF----NQVSKPDaqqvDFSAIVKLLEQ 283
Cdd:PLN02858  242 VLVQNLGIVLDMAKSLPFPLPLLAVAHQQLisgsSSMQGDD----TATSLAKVWEK 293
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 3-64 1.10e-07

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 52.49  E-value: 1.10e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488044815   3 QSVSFIGLGAMGWHMASHLTQV-CSQVYVWNRTFAKAKQHEQTFGTQAV---DLTQAL-QADIIFSC 64
Cdd:PRK00045 183 KKVLVIGAGEMGELVAKHLAEKgVRKITVANRTLERAEELAEEFGGEAIpldELPEALaEADIVISS 249
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 3-64 1.76e-07

Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440142 [Multi-domain]  Cd Length: 425  Bit Score: 52.04  E-value: 1.76e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488044815   3 QSVSFIGLGAMGWHMASHLTQV-CSQVYVWNRTFAKAKQHEQTFGTQAV---DLTQAL-QADIIFSC 64
Cdd:COG0373  183 KTVLVIGAGEMGELAARHLAAKgVKRITVANRTLERAEELAEEFGGEAVpleELPEALaEADIVISS 249
PLN02350 PLN02350
phosphogluconate dehydrogenase (decarboxylating)
 9-191 4.00e-06

phosphogluconate dehydrogenase (decarboxylating)


Pssm-ID: 215200 [Multi-domain]  Cd Length: 493  Bit Score: 47.79  E-value: 4.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   9 GLGAMGWHMASHLTQVCSQVYVWNRTFAK-------AKQ--HEQTFGTQAV-DLTQALQAD---IIF--SCLPTSQDVEN 73
Cdd:PLN02350  13 GLAVMGQNLALNIAEKGFPISVYNRTTSKvdetverAKKegNLPLYGFKDPeDFVLSIQKPrsvIILvkAGAPVDQTIKA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815  74 LiadSQ-LKQGCIWVDCTSGVPETARKLSQQLKVNGVDYLDAPVSGQTIGAERGTlTVMVGGDESAFKRAKPIIQAFANL 152
Cdd:PLN02350  93 L---SEyMEPGDCIIDGGNEWYENTERRIKEAAEKGLLYLGMGVSGGEEGARNGP-SLMPGGSFEAYKNIEDILEKVAAQ 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 488044815 153 VE------YVGESGAAFAVKAINNTLMATHLWALAEGLSILKSQG 191
Cdd:PLN02350 169 VDdgpcvtYIGPGGAGNFVKMVHNGIEYGDMQLISEAYDVLKSVG 213
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 4-192 1.26e-05

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


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 45.57  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   4 SVSFIGLGAMGWHMASHLT----QVcsqVYVWNRTFAKAKQHEQTFGTQAVDLTQAL--QADIIFSCLPtsqD------V 71
Cdd:COG5495    5 KIGIIGAGRVGTALAAALRaaghEV---VGVYSRSPASAERAAALLGAVPALDLEELaaEADLVLLAVP---DdaiaevA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815  72 ENLIADSQLKQGCIWVDCtSG-VP-ETARKLSQQLKVNGVDYldaPVsgQTIGAERGTLTVMVG------GDESAFKRAK 143
Cdd:COG5495   79 AGLAAAGALRPGQLVVHT-SGaLGsDVLAPAARAGALTGSFH---PL--QTFSGPREDLERLAGipfaieGDEEALPVLE 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488044815 144 PIIQAFANLVEYVGES-------GAAFAvkaiNNTLMatHLWALAEglSILKSQGV 192
Cdd:COG5495  153 ALAEALGGEPFVIDSEqrplyhaAAVFA----SNFLV--TLVALAA--ELLEAAGL 200
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 8-191 4.18e-05

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 44.78  E-value: 4.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   8 IGLGAMGWHMASHLTQVCSQVYVWNRTFAK--------AKQHEQTFGTQAVD-LTQALQAD-----IIFSCLPTSQDVEN 73
Cdd:PTZ00142   7 IGLAVMGQNLALNIASRGFKISVYNRTYEKteefvkkaKEGNTRVKGYHTLEeLVNSLKKPrkvilLIKAGEAVDETIDN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815  74 LIadSQLKQGCIWVDCTSGVPETARKLSQQLKVNGVDYLDAPVSGQTIGAERGTlTVMVGGDESAFKRAKPIIQAFA--- 150
Cdd:PTZ00142  87 LL--PLLEKGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGP-SLMPGGNKEAYDHVKDILEKCSakv 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 488044815 151 ---NLVEYVGESGAAFAVKAINNTLMATHLWALAEGLSILKSQG 191
Cdd:PTZ00142 164 gdsPCVTYVGPGSSGHYVKMVHNGIEYGDMQLISESYKLMKHIL 207
PRK14619 PRK14619
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
 1-150 7.61e-05

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237771 [Multi-domain]  Cd Length: 308  Bit Score: 43.44  E-value: 7.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   1 MIQSVSFIGLGAMGWHMASHLTQVCSQVYVWNRtfakakqheqtfgTQAVDLTQALQ-ADIIFSCLPTS--QDVENLIAD 77
Cdd:PRK14619   3 QPKTIAILGAGAWGSTLAGLASANGHRVRVWSR-------------RSGLSLAAVLAdADVIVSAVSMKgvRPVAEQVQA 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488044815  78 SQLKQGCIWVDCTSGV-PETARKLSQQLKVNGVDYLDAPVSGQTIGAE-RGTL---TVMVGGDESAfkrAKPIIQAFA 150
Cdd:PRK14619  70 LNLPPETIIVTATKGLdPETTRTPSQIWQAAFPNHPVVVLSGPNLSKEiQQGLpaaTVVASRDLAA---AETVQQIFS 144
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-94 1.24e-04

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: 42.74  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   1 MIQSVSFIGLGAMGWHMASHLTQ---VCSQVYVWNRTFAKAKQHEQTFGTQAV-DLTQAL-QADIIFSCLPTsQDVENLI 75
Cdd:COG0345    1 MSMKIGFIGAGNMGSAIIKGLLKsgvPPEDIIVSDRSPERLEALAERYGVRVTtDNAEAAaQADVVVLAVKP-QDLAEVL 79

                         90       100
                 ....*....|....*....|.
gi 488044815  76 AD--SQLKQGCIWVDCTSGVP 94
Cdd:COG0345   80 EElaPLLDPDKLVISIAAGVT 100
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 5-64 1.46e-04

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (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: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 42.64  E-value: 1.46e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488044815   5 VSFIGLGAMGWHMASHLTQV-CSQVYVWNRTFAKAKQHEQTFGTQAVDLTQAL----QADIIFSC 64
Cdd:cd05213  181 VLVIGAGEMGELAAKHLAAKgVAEITIANRTYERAEELAKELGGNAVPLDELLellnEADVVISA 245
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 5-88 1.70e-04

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 40.63  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815    5 VSFIGLGAMGWHMASHL-TQVCSQVYVWNRTFAKAKQ-HEQTFGTQAVDLTQAL----QADIIFSC------LPTSQDVE 72
Cdd:pfam01488  15 VLLIGAGEMGELVAKHLlAKGAKEVTIANRTIERAQElAEKFGGVEALPLDDLKeylaEADIVISAtssptpIITKEMVE 94

                          90
                  ....*....|....*.
gi 488044815   73 NliADSQLKQGCIWVD 88
Cdd:pfam01488  95 R--ALKPRKKPLLFVD 108
PRK09287 PRK09287
NADP-dependent phosphogluconate dehydrogenase;
102-170 2.60e-04

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236453 [Multi-domain]  Cd Length: 459  Bit Score: 42.03  E-value: 2.60e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488044815 102 QQLKVNGVDYLDAPVSGQTIGAERGTlTVMVGGDESAFKRAKPIIQAFANLVE-------YVGESGAAFAVKAINN 170
Cdd:PRK09287 101 KELAEKGIHFIGMGVSGGEEGALHGP-SIMPGGQKEAYELVAPILEKIAAKVEdgepcvtYIGPDGAGHYVKMVHN 175
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 8-82 5.47e-04

D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.


Pssm-ID: 427007 [Multi-domain]  Cd Length: 178  Bit Score: 39.79  E-value: 5.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488044815    8 IGLGAMGWHMASHLTQVCSQVYVWNRTfAKAKQHEQTFGTQAVDLTQAL-QADIIFSCLPTSQDVENLIADSQLKQ 82
Cdd:pfam02826  42 IGLGRIGRAVAKRLKAFGMKVIAYDRY-PKPEEEEEELGARYVSLDELLaESDVVSLHLPLTPETRHLINAERLAL 116
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
 5-97 1.87e-03

Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the D-specific 2-hydroxyacid dehydrogenase family, catalyzes the NAD-dependent formation of phosphate from phosphite (hydrogen phosphonate). PTDH has been suggested as a potential enzyme for cofactor regeneration systems. The D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD-binding domain.


Pssm-ID: 240634 [Multi-domain]  Cd Length: 318  Bit Score: 39.19  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488044815   5 VSFIGLGAMGWHMASHLTQVCSQVYVWNRTfAKAKQHEQTFGTQAVDLTQAL-QADIIFSCLPTSQDVENLIADSQL--- 80
Cdd:cd12157  147 VGILGMGALGRAIARRLSGFGATLLYYDPH-PLDQAEEQALNLRRVELDELLeSSDFLVLALPLTPDTLHLINAEALakm 225

                         90
                 ....*....|....*....
gi 488044815  81 KQGCIWVDCTSG--VPETA 97
Cdd:cd12157  226 KPGALLVNPCRGsvVDEAA 244
 
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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