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Conserved domains on  [gi|2485516090|ref|WP_278349871|]
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MULTISPECIES: 3-hydroxyisobutyrate dehydrogenase [Marinobacter]

Protein Classification

3-hydroxyisobutyrate dehydrogenase( domain architecture ID 11493045)

3-hydroxyisobutyrate dehydrogenase (HIBADH) catalyzes the conversion from 3-hydroxy-2-methylpropanoate and NAD(+) to 2-methyl-3-oxopropanoate and NADH

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 6-293 9.19e-142

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: 400.71  E-value: 9.19e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   6 FIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGARTADSGKAAAEGAECVITMLPAGKHVEAVYLGDDGLLAAL 85
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  86 PAGTLVIDSSTIAPETARNVAEQAAERKLAFIDAPVSGGVGGAKAGTLTFICGGDASTFEKAKPILEGMGKNIFHAGPHG 165
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090 166 AGQVAKICNNMLLAILMAGTSEALALGAKNGLDPAVLSEIMKQSSGGNWALNVYNPWPGVMEGVPASRDYQGGFLVNLMA 245
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVPGVMPQAPASNGYQGGFGTALML 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2485516090 246 KDLGLAFDNAVTNQASIPMGSLARNLFQLHAGQGNGELDFSSILRLYK 293
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLLR 288
 
Name Accession Description Interval E-value
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 6-293 9.19e-142

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: 400.71  E-value: 9.19e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   6 FIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGARTADSGKAAAEGAECVITMLPAGKHVEAVYLGDDGLLAAL 85
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  86 PAGTLVIDSSTIAPETARNVAEQAAERKLAFIDAPVSGGVGGAKAGTLTFICGGDASTFEKAKPILEGMGKNIFHAGPHG 165
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090 166 AGQVAKICNNMLLAILMAGTSEALALGAKNGLDPAVLSEIMKQSSGGNWALNVYNPWPGVMEGVPASRDYQGGFLVNLMA 245
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVPGVMPQAPASNGYQGGFGTALML 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2485516090 246 KDLGLAFDNAVTNQASIPMGSLARNLFQLHAGQGNGELDFSSILRLYK 293
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLLR 288
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-292 1.36e-129

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 369.83  E-value: 1.36e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   1 MAKITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGARTADSGKAAAEGAECVITMLPAGKHVEAVYLGDDG 80
Cdd:COG2084     1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  81 LLAALPAGTLVIDSSTIAPETARNVAEQAAERKLAFIDAPVSGGVGGAKAGTLTFICGGDASTFEKAKPILEGMGKNIFH 160
Cdd:COG2084    81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090 161 AGPHGAGQVAKICNNMLLAILMAGTSEALALGAKNGLDPAVLSEIMKQSSGGNWALNVYNPWpgvmegvPASRDYQGGFL 240
Cdd:COG2084   161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPR-------MLAGDFDPGFA 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2485516090 241 VNLMAKDLGLAFDNAVTNQASIPMGSLARNLFQLHAGQGNGELDFSSILRLY 292
Cdd:COG2084   234 LDLMLKDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-292 2.28e-77

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 237.26  E-value: 2.28e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   1 MAKITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGARTADSGKAAAEGAECVITMLPAGKHVEAVYLGDDG 80
Cdd:PRK11559    2 TMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  81 LLAALPAGTLVIDSSTIAPETARNVAEQAAERKLAFIDAPVSGGVGGAKAGTLTFICGGDASTFEKAKPILEGMGKNIFH 160
Cdd:PRK11559   82 IIEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090 161 AGPHGAGQVAKICNNMLLAILMAGTSEALALGAKNGLDPAVLSEIMKQSSGGNWALNVYNPWpgVMEgvpasRDYQGGFL 240
Cdd:PRK11559  162 TGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPM--VMD-----RNFKPGFR 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2485516090 241 VNLMAKDLGLAFDNAVTNQASIPMGSLARNLFQLHAGQGNGELDFSSILRLY 292
Cdd:PRK11559  235 IDLHIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYY 286
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 3-162 4.55e-73

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: 221.57  E-value: 4.55e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   3 KITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGARTADSGKAAAEGAECVITMLPAGKHVEAVYLGDdGLL 82
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  83 AALPAGTLVIDSSTIAPETARNVAEQAAERKLAFIDAPVSGGVGGAKAGTLTFICGGDASTFEKAKPILEGMGKNIFHAG 162
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
 4-114 9.99e-04

atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is related to, but is different from, the archetypical SDRs, GXGXXG. This subgroup also lacks most of the characteristic active site residues of the SDRs; however, the upstream Ser is present at the usual place, and some potential catalytic residues are present in place of the usual YXXXK active site motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187576 [Multi-domain]  Cd Length: 251  Bit Score: 40.00  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   4 ITFIGLGNMGAPMAANLLKAGHDVTV--------FDLSQPAVEALVAEGARTADSGKAAA-----------------EGA 58
Cdd:cd05266     1 VLILGCGYLGQRLARQLLAQGWQVTGttrspeklAADRPAGVTPLAADLTQPGLLADVDHlvislpppagsyrggydPGL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485516090  59 ECVITMLPAGKHVE--------AVYlGDDGllaalpaGTLVIDSSTIAPETARNVAEQAAERKL 114
Cdd:cd05266    81 RALLDALAQLPAVQrviylsstGVY-GDQQ-------GEWVDETSPPNPSTESGRALLEAEQAL 136
 
Name Accession Description Interval E-value
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 6-293 9.19e-142

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: 400.71  E-value: 9.19e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   6 FIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGARTADSGKAAAEGAECVITMLPAGKHVEAVYLGDDGLLAAL 85
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  86 PAGTLVIDSSTIAPETARNVAEQAAERKLAFIDAPVSGGVGGAKAGTLTFICGGDASTFEKAKPILEGMGKNIFHAGPHG 165
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090 166 AGQVAKICNNMLLAILMAGTSEALALGAKNGLDPAVLSEIMKQSSGGNWALNVYNPWPGVMEGVPASRDYQGGFLVNLMA 245
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVPGVMPQAPASNGYQGGFGTALML 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2485516090 246 KDLGLAFDNAVTNQASIPMGSLARNLFQLHAGQGNGELDFSSILRLYK 293
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLLR 288
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-292 1.36e-129

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 369.83  E-value: 1.36e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   1 MAKITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGARTADSGKAAAEGAECVITMLPAGKHVEAVYLGDDG 80
Cdd:COG2084     1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  81 LLAALPAGTLVIDSSTIAPETARNVAEQAAERKLAFIDAPVSGGVGGAKAGTLTFICGGDASTFEKAKPILEGMGKNIFH 160
Cdd:COG2084    81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090 161 AGPHGAGQVAKICNNMLLAILMAGTSEALALGAKNGLDPAVLSEIMKQSSGGNWALNVYNPWpgvmegvPASRDYQGGFL 240
Cdd:COG2084   161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPR-------MLAGDFDPGFA 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2485516090 241 VNLMAKDLGLAFDNAVTNQASIPMGSLARNLFQLHAGQGNGELDFSSILRLY 292
Cdd:COG2084   234 LDLMLKDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-292 2.28e-77

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 237.26  E-value: 2.28e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   1 MAKITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGARTADSGKAAAEGAECVITMLPAGKHVEAVYLGDDG 80
Cdd:PRK11559    2 TMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  81 LLAALPAGTLVIDSSTIAPETARNVAEQAAERKLAFIDAPVSGGVGGAKAGTLTFICGGDASTFEKAKPILEGMGKNIFH 160
Cdd:PRK11559   82 IIEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090 161 AGPHGAGQVAKICNNMLLAILMAGTSEALALGAKNGLDPAVLSEIMKQSSGGNWALNVYNPWpgVMEgvpasRDYQGGFL 240
Cdd:PRK11559  162 TGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPM--VMD-----RNFKPGFR 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2485516090 241 VNLMAKDLGLAFDNAVTNQASIPMGSLARNLFQLHAGQGNGELDFSSILRLY 292
Cdd:PRK11559  235 IDLHIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYY 286
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 3-162 4.55e-73

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: 221.57  E-value: 4.55e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   3 KITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGARTADSGKAAAEGAECVITMLPAGKHVEAVYLGDdGLL 82
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  83 AALPAGTLVIDSSTIAPETARNVAEQAAERKLAFIDAPVSGGVGGAKAGTLTFICGGDASTFEKAKPILEGMGKNIFHAG 162
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 3-293 1.37e-71

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: 222.46  E-value: 1.37e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   3 KITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGARTADSGKAAAEGAECVITMLPAGKHVEAVYLGDDGLL 82
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  83 AALPAGTLVIDSSTIAPETARNVAEQAAERKLAFIDAPVSGGVGGAKAGTLTFICGGDASTFEKAKPILEGMGKNIFHAG 162
Cdd:TIGR01505  81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090 163 PHGAGQVAKICNNMLLAILMAGTSEALALGAKNGLDPAVLSEIMKQSSGGNWALNVYNPwpgvmegVPASRDYQGGFLVN 242
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGE-------RVIDRTFKPGFRID 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2485516090 243 LMAKDLGLAFDNAVTNQASIPMGSLARNLFQLHAGQGNGELDFSSILRLYK 293
Cdd:TIGR01505 234 LHQKDLNLALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALE 284
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
1-289 2.67e-66

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 209.33  E-value: 2.67e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   1 MAKITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGARTADSGKAAAEGAECVITMLPAGKHVEAVYLGDDG 80
Cdd:PRK15461    1 MAAIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  81 LLAALPAGTLVIDSSTIAPETARNVAEQAAERKLAFIDAPVSGGVGGAKAGTLTFICGGDASTFEKAKPILEGMGKNIFH 160
Cdd:PRK15461   81 VCEGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090 161 AGPHGAGQVAKICNNMLLAILMAGTSEALALGAKNGLDPAVLSEIMKQSSGGNWALNVynPWPG-VMEGvpasrDYQGGF 239
Cdd:PRK15461  161 AGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALGLSFDVALKVMSGTAAGKGHFTT--TWPNkVLKG-----DLSPAF 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2485516090 240 LVNLMAKDLGLAFDNAVTNQASIPMGSLARNLFQLHAGQGNGELDFSSIL 289
Cdd:PRK15461  234 MIDLAHKDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAIL 283
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
3-290 2.33e-49

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 165.58  E-value: 2.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   3 KITFIGLGNMGAPMAANLLKAGHDVTVFDLSqPAVEALVAEGARTADSGKAAAEGAECVITMLPAGKHVEAVYLGDDGLL 82
Cdd:PRK15059    2 KLGFIGLGIMGTPMAINLARAGHQLHVTTIG-PVADELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  83 AALPAGTLVIDSSTIAPETARNVAEQAAERKLAFIDAPVSGGVGGAKAGTLTFICGGDASTFEKAKPILEGMGKNIFHAG 162
Cdd:PRK15059   81 KASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090 163 PHGAGQVAKICNNMLLAILMAGTSEALALGAKNGLDPAVLSEIMKQSSGGNWALNVYNPwpgvmegVPASRDYQGGFLVN 242
Cdd:PRK15059  161 GNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGE-------RMIKRTFNPGFKIA 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2485516090 243 LMAKDLGLAFDNAVTNQASIPMGSLARNLFQLHAGQGNGELDFSSILR 290
Cdd:PRK15059  234 LHQKDLNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQ 281
PLN02858 PLN02858
fructose-bisphosphate aldolase
 3-293 2.99e-43

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 158.09  E-value: 2.99e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090    3 KITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGARTADSGKAAAEGAECVITMLPAGKHVEAVYLGDDGLL 82
Cdd:PLN02858   326 RIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAV 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   83 AALPAGTLVIDSSTIAPETARNVAE--QAAERKLAFIDAPVSGGVGGAKAGTLTFICGGDASTFEKAKPILEGMGKNI-F 159
Cdd:PLN02858   406 SALPAGASIVLSSTVSPGFVIQLERrlENEGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKLyV 485

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  160 HAGPHGAGQVAKICNNMLLAILMAGTSEALALGAKNGLDPAVLSEIMKQSSGGNWALNvyNPWPGVMEGvpasrDYQGGF 239
Cdd:PLN02858   486 IKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFE--NRVPHMLDN-----DYTPYS 558

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2485516090  240 LVNLMAKDLGLAFDNAVTNQASIPMGSLARNLFQLHAGQGNGELDFSSILRLYK 293
Cdd:PLN02858   559 ALDIFVKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVYE 612
PLN02858 PLN02858
fructose-bisphosphate aldolase
 2-293 2.61e-39

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 146.54  E-value: 2.61e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090    2 AKITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGARTADSGKAAAEGAECVITMLPAGKHVEAVYLGDDGL 81
Cdd:PLN02858     5 GVVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFGDEGA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   82 LAALPAGTLVIDSSTIAPETARNVAEQAAERK--LAFIDAPVSGGVGGAKAGTLTFICGGDASTFEKAKPILEGMGKNIF 159
Cdd:PLN02858    85 AKGLQKGAVILIRSTILPLQLQKLEKKLTERKeqIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKLY 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  160 HA-GPHGAGQVAKICNNMLLAILMAGTSEALALGAKNGLDPAVLSEIMKQSSGGNWALnvYNPWPGVMEGVPASRDYqgg 238
Cdd:PLN02858   165 TFeGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIF--KNHVPLLLKDDYIEGRF--- 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2485516090  239 flVNLMAKDLGLAFDNAVTNQASIPMGSLARNLFQLHAGQGNGELDFSSILRLYK 293
Cdd:PLN02858   240 --LNVLVQNLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKVWE 292
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 165-292 1.01e-35

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: 124.56  E-value: 1.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090 165 GAGQVAKICNNMLLAILMAGTSEALALGAKNGLDPAVLSEIMKQSSGGNWALnvynpwPGVMEGVPASRDYQGGFLVNLM 244
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNAL------ENKFPQRVLSRDFDPGFALDLM 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2485516090 245 AKDLGLAFDNAVTNQASIPMGSLARNLFQLHAGQGNGELDFSSILRLY 292
Cdd:pfam14833  75 LKDLGLALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
YqeC COG1023
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
3-171 1.86e-33

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


Pssm-ID: 440646 [Multi-domain]  Cd Length: 300  Bit Score: 124.05  E-value: 1.86e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   3 KITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGARTADSGKAAAEGAE---CVITMLPAGKHVEAVYlgdD 79
Cdd:COG1023     2 QIGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKLPaprVVWLMVPAGEITDQVI---E 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  80 GLLAALPAGTLVIDSS-TIAPETARNvAEQAAERKLAFIDAPVSGGVGGAKAGtLTFICGGDASTFEKAKPILE----GM 154
Cdd:COG1023    79 ELAPLLEPGDIVIDGGnSNYKDDIRR-AEELAEKGIHFVDVGTSGGVWGLENG-YCLMIGGDKEAVERLEPIFKalapGA 156

                         170
                  ....*....|....*..
gi 2485516090 155 GKNIFHAGPHGAGQVAK 171
Cdd:COG1023   157 ENGYLHCGPVGAGHFVK 173
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
3-171 1.11e-31

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 119.47  E-value: 1.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   3 KITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGARTADSGK--AAAEGAECVI-TMLPAGKHVEAVYlgdD 79
Cdd:PRK09599    2 QLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEelVAKLPAPRVVwLMVPAGEITDATI---D 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  80 GLLAALPAGTLVIDS-STIAPETARNvAEQAAERKLAFIDAPVSGGVGGAKAGTLTFIcGGDASTFEKAKPILE----GM 154
Cdd:PRK09599   79 ELAPLLSPGDIVIDGgNSYYKDDIRR-AELLAEKGIHFVDVGTSGGVWGLERGYCLMI-GGDKEAVERLEPIFKalapRA 156

                         170
                  ....*....|....*..
gi 2485516090 155 GKNIFHAGPHGAGQVAK 171
Cdd:PRK09599  157 EDGYLHAGPVGAGHFVK 173
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 1-219 4.86e-09

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 56.72  E-value: 4.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   1 MAKITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAegartadsgKAAAEGAEC------------------VI 62
Cdd:PTZ00142    1 MSDIGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEEFVK---------KAKEGNTRVkgyhtleelvnslkkprkVI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  63 TMLPAGKHVEAVYlgdDGLLAALPAGTLVIDSSTIAPETARNVAEQAAERKLAFIDAPVSGGVGGAKAGTlTFICGGDAS 142
Cdd:PTZ00142   72 LLIKAGEAVDETI---DNLLPLLEKGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGP-SLMPGGNKE 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090 143 TFEKAKPILE------GMGKNIFHAGPHGAGQVAKICNNMLLAILMAGTSEA-LALGAKNGLDPAVLSEIMKQSSGGNwa 215
Cdd:PTZ00142  148 AYDHVKDILEkcsakvGDSPCVTYVGPGSSGHYVKMVHNGIEYGDMQLISESyKLMKHILGMSNEELSEVFNKWNEGI-- 225


                  ....
gi 2485516090 216 LNVY 219
Cdd:PTZ00142  226 LNSY 229
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-92 2.10e-08

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: 53.91  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   1 MAKITFIGLGNMGAPMAANLLKAG---HDVTVFDLSQPAVEALVAE-GARTADSGKAAAEGAECVI-TMLPagKHVEAVy 75
Cdd:COG0345     2 SMKIGFIGAGNMGSAIIKGLLKSGvppEDIIVSDRSPERLEALAERyGVRVTTDNAEAAAQADVVVlAVKP--QDLAEV- 78

                          90
                  ....*....|....*..
gi 2485516090  76 lgDDGLLAALPAGTLVI 92
Cdd:COG0345    79 --LEELAPLLDPDKLVI 93
PRK09287 PRK09287
NADP-dependent phosphogluconate dehydrogenase;
12-167 1.21e-07

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236453 [Multi-domain]  Cd Length: 459  Bit Score: 52.43  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  12 MGAPMAANLLKAGHDVTVFDLSQPAVEALVAE--------GARTADSGKAAAEGAECVITMLPAGKHVEAVYlgdDGLLA 83
Cdd:PRK09287    1 MGKNLALNIASHGYTVAVYNRTPEKTDEFLAEegkgkkivPAYTLEEFVASLEKPRKILLMVKAGAPVDAVI---EQLLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  84 ALPAGTLVIDS-STIAPETARNVAEqAAERKLAFIDAPVSGGVGGAKAGTlTFICGGDASTFEKAKPILEGMGKNIF--- 159
Cdd:PRK09287   78 LLEKGDIIIDGgNSNYKDTIRREKE-LAEKGIHFIGMGVSGGEEGALHGP-SIMPGGQKEAYELVAPILEKIAAKVEdge 155

                         170
                  ....*....|..
gi 2485516090 160 ----HAGPHGAG 167
Cdd:PRK09287  156 pcvtYIGPDGAG 167
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 3-112 2.26e-07

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: 51.46  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   3 KITFIGLGNMGAPMAANLLKAGHDVTVFDLSQ---------------PAVEALVAEGARTA-----DSGKAAAEGAE--- 59
Cdd:TIGR03026   2 KIAVIGLGYVGLPLAALLADLGHDVTGVDIDQekvdklnkgkspiyePGLDELLAKALKAGrlratTDYEEAIRDADvii 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516090  60 -CVITMLPAGKHVEAVYLGD--DGLLAALPAGTLVIDSSTIAPETARNVAEQAAER 112
Cdd:TIGR03026  82 iCVPTPLKEDGSPDLSYVESaaETIAKHLRKGATVVLESTVPPGTTEEVVKPILER 137
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
4-163 5.92e-07

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 49.01  E-value: 5.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   4 ITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGARTADSG--KAAAEGAECVITMLPAGKHVEAVYLGDDGL 81
Cdd:COG2085     1 IGIIGTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAELGPGARAGtnAEAAAAADVVVLAVPYEAVPDVLESLGDAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  82 laalpAGTLVIDSS-----------TIAPET--ARNVAEQAAERKL--AF--IDAPVSGGVGGAKAGTLT-FICGGDAST 143
Cdd:COG2085    81 -----AGKIVIDATnplperdgfilDPPGGGsaAELVAALLPGARVvkAFntIGAAVLADPARPAGGRRDvFVAGDDAEA 155

                         170       180
                  ....*....|....*....|
gi 2485516090 144 FEKAKPILEGMGKNIFHAGP 163
Cdd:COG2085   156 KAVVAALIEDLGFDPVDAGP 175
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-62 6.17e-07

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 49.76  E-value: 6.17e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516090   1 MAKITFIGLGNMGAPMAANLLKAG---HDVTVFDLSQPAVEALVAE-GARTADSGKAAAEGAECVI 62
Cdd:PRK11880    2 MKKIGFIGGGNMASAIIGGLLASGvpaKDIIVSDPSPEKRAALAEEyGVRAATDNQEAAQEADVVV 67
PLN02350 PLN02350
phosphogluconate dehydrogenase (decarboxylating)
 2-175 1.78e-06

phosphogluconate dehydrogenase (decarboxylating)


Pssm-ID: 215200 [Multi-domain]  Cd Length: 493  Bit Score: 48.94  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   2 AKITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAegaRTADSGKAAAEGAE-------------CVITMLPAG 68
Cdd:PLN02350    7 SRIGLAGLAVMGQNLALNIAEKGFPISVYNRTTSKVDETVE---RAKKEGNLPLYGFKdpedfvlsiqkprSVIILVKAG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  69 KHVEAVYlgdDGLLAALPAGTLVIDSSTIAPETARNVAEQAAERKLAFIDAPVSGGVGGAKAGTlTFICGGDASTFEKAK 148
Cdd:PLN02350   84 APVDQTI---KALSEYMEPGDCIIDGGNEWYENTERRIKEAAEKGLLYLGMGVSGGEEGARNGP-SLMPGGSFEAYKNIE 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2485516090 149 PILEGM------GKNIFHAGPHGAGQVAKICNN 175
Cdd:PLN02350  160 DILEKVaaqvddGPCVTYIGPGGAGNFVKMVHN 192
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
 2-111 2.29e-06

UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 397677 [Multi-domain]  Cd Length: 186  Bit Score: 47.24  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   2 AKITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEAL--------------VAEGAR------TADSGKAAAEGAE-- 59
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLnsgqipiyepgldeLVKANVsgrlsfTTDYSTAIEEADVif 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516090  60 -CVIT------MLPAGKHVEAVYlgdDGLLAALPAGTLVIDSSTIAPETARNVAEQAAE 111
Cdd:pfam03721  81 iAVGTpskkggGAADLKYVESAA---RSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIE 136
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 1-164 3.62e-06

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: 47.43  E-value: 3.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   1 MAKITFIGLGNMGAPMAANLLKAG--HDVTVFDLSQPAVEALVAEGA--RTADSGKAAAEGAECVITMLPAGKHVEAVyl 76
Cdd:COG0287     1 FMRIAIIGLGLIGGSLALALKRAGlaHEVVGVDRSPETLERALELGVidRAATDLEEAVADADLVVLAVPVGATIEVL-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  77 gdDGLLAALPAGTLVID-SSTIAPetarnVAEQAAE---RKLAFIDA-PVSG----GVGGAKAG-------TLTFICGGD 140
Cdd:COG0287    79 --AELAPHLKPGAIVTDvGSVKGA-----VVEAAEAllpDGVRFVGGhPMAGteksGPEAADADlfegapyILTPTEGTD 151

                         170       180
                  ....*....|....*....|....
gi 2485516090 141 ASTFEKAKPILEGMGKNIFHAGPH 164
Cdd:COG0287   152 PEALERVEELWEALGARVVEMDPE 175
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 1-59 6.78e-05

3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440862 [Multi-domain]  Cd Length: 281  Bit Score: 43.56  E-value: 6.78e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516090   1 MAKITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEA----LVAEGARTADSGKAAAEGAE 59
Cdd:COG1250     2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERararIAKLLDKLVKKGKLTEEEAD 64
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
3-111 7.54e-05

UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 43.86  E-value: 7.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   3 KITFIGLGNMGAPMAANLLKAGHDVTVFD--------LSQ-------PAVEALVAEGARTA-----DSGKAAAEGAE--- 59
Cdd:COG1004     2 KIAVIGTGYVGLVTAACLAELGHEVTCVDideekieaLNAgeipiyePGLEELVARNVAAGrlrftTDLAEAVAEADvvf 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  60 -CVITmlPAG-------KHVEAVYlgdDGLLAALPAGTLVIDSSTIAPETARNVAEQAAE 111
Cdd:COG1004    82 iAVGT--PSDedgsadlSYVLAAA---RSIGEALKGYKVVVTKSTVPVGTADRVRAIIAE 136
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 3-46 1.78e-04

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 42.53  E-value: 1.78e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2485516090   3 KITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGAR 46
Cdd:PRK06522    2 KIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLR 45
PRK07502 PRK07502
prephenate/arogenate dehydrogenase family protein;
3-212 3.58e-04

prephenate/arogenate dehydrogenase family protein;


Pssm-ID: 236034 [Multi-domain]  Cd Length: 307  Bit Score: 41.49  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   3 KITFIGLGNMGAPMAANLLKAG--HDVTVFDLSqPAVEALVAE---GARTADSGKAAAEGAECVITMLPAGKHVEAVylg 77
Cdd:PRK07502    8 RVALIGIGLIGSSLARAIRRLGlaGEIVGADRS-AETRARARElglGDRVTTSAAEAVKGADLVILCVPVGASGAVA--- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090  78 dDGLLAALPAGTLVIDSSTIAPETARNVAEQAAErKLAFIDA-PVSGGV-GGAKAG----------TLTFICGGDASTFE 145
Cdd:PRK07502   84 -AEIAPHLKPGAIVTDVGSVKASVIAAMAPHLPE-GVHFIPGhPLAGTEhSGPDAGfaelfenrwcILTPPEGTDPAAVA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516090 146 KAKPILEGMGKNIFHAGPHGAGQVAKICNNM--LLAILMAGTSEALALGAKngldpavlSEIMKQSSGG 212
Cdd:PRK07502  162 RLTAFWRALGARVEEMDPEHHDLVLAITSHLphLIAYTIVGTADDLERVTE--------SEVIKYSASG 222
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 3-92 4.79e-04

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 41.00  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   3 KITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAvEALVAEGAR-------------TADSGKAAAEGAECVITMLPAGK 69
Cdd:COG1893     2 KIAILGAGAIGGLLGARLARAGHDVTLVARGAHA-EALRENGLRlespdgdrttvpvPAVTDPEELGPADLVLVAVKAYD 80

                          90       100
                  ....*....|....*....|...
gi 2485516090  70 HVEAVylgdDGLLAALPAGTLVI 92
Cdd:COG1893    81 LEAAA----EALAPLLGPDTVVL 99
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 4-94 6.07e-04

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 40.91  E-value: 6.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   4 ITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVE--ALVAEGARTADSGKAAAEGAECVITMlpagkhveavylgDDGL 81
Cdd:PRK06130    7 LAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALEraRGVIERALGVYAPLGIASAGMGRIRM-------------EAGL 73

                          90
                  ....*....|...
gi 2485516090  82 LAALPAGTLVIDS 94
Cdd:PRK06130   74 AAAVSGADLVIEA 86
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 3-47 9.59e-04

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: 40.05  E-value: 9.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2485516090   3 KITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGART 47
Cdd:COG0569    97 HVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLV 141
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
 4-114 9.99e-04

atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is related to, but is different from, the archetypical SDRs, GXGXXG. This subgroup also lacks most of the characteristic active site residues of the SDRs; however, the upstream Ser is present at the usual place, and some potential catalytic residues are present in place of the usual YXXXK active site motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187576 [Multi-domain]  Cd Length: 251  Bit Score: 40.00  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   4 ITFIGLGNMGAPMAANLLKAGHDVTV--------FDLSQPAVEALVAEGARTADSGKAAA-----------------EGA 58
Cdd:cd05266     1 VLILGCGYLGQRLARQLLAQGWQVTGttrspeklAADRPAGVTPLAADLTQPGLLADVDHlvislpppagsyrggydPGL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485516090  59 ECVITMLPAGKHVE--------AVYlGDDGllaalpaGTLVIDSSTIAPETARNVAEQAAERKL 114
Cdd:cd05266    81 RALLDALAQLPAVQrviylsstGVY-GDQQ-------GEWVDETSPPNPSTESGRALLEAEQAL 136
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 3-56 1.86e-03

3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 38.29  E-value: 1.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485516090   3 KITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEA-----------LVAEGARTADSGKAAAE 56
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKaleriesslerLVEKGRITEEEVDAALA 65
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
8-62 4.69e-03

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 38.04  E-value: 4.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516090   8 GLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGA--------RTADSGKAAAEGAECVI 62
Cdd:COG0451     7 GAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGvefvrgdlRDPEALAAALAGVDAVV 69
PRK07819 PRK07819
3-hydroxybutyryl-CoA dehydrogenase; Validated
 1-59 5.87e-03

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181133 [Multi-domain]  Cd Length: 286  Bit Score: 37.66  E-value: 5.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516090   1 MAKITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEA----LVAEGARTADSGKAAAEGAE 59
Cdd:PRK07819    5 IQRVGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAgrnrIEKSLERAVSRGKLTERERD 67
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-62 7.72e-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: 37.10  E-value: 7.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485516090   1 MAKITFIGLGNMGAPMAANLLKAGHDVT-VFDLSQPAVEALVAE-GARTADSGKAAAEGAECVI 62
Cdd:COG5495     3 RMKIGIIGAGRVGTALAAALRAAGHEVVgVYSRSPASAERAAALlGAVPALDLEELAAEADLVL 66
PRK09260 PRK09260
3-hydroxyacyl-CoA dehydrogenase;
1-86 8.26e-03

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 236434 [Multi-domain]  Cd Length: 288  Bit Score: 37.08  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516090   1 MAKITFIGLGNMGAPMAANLLKAGHDVTVFDLSQPAVEALVAEGARTADS----GKAAAEGAECVITMLPAGKHVEAVYL 76
Cdd:PRK09260    1 IEKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQgvarGKLTEAARQAALARLSYSLDLKAAVA 80

                          90
                  ....*....|
gi 2485516090  77 GDDGLLAALP 86
Cdd:PRK09260   81 DADLVIEAVP 90
 
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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