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Conserved domains on  [gi|1003328269|gb|AMO37487|]
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2-hydroxy-3-oxopropionate reductase [Thauera humireducens]

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 ...
 1-284 2.17e-110

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


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 320.91  E-value: 2.17e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPLYATPAELAARSEVVITIVTASADVDALAFGPDGL 80
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  81 AAGFAPGAIHVDMSTIAPAMARSLAERHAARGIGFVDAPVSGGGQGARDATLAIMAGAEADVLERVRPLLAAMGKRIVHI 160
Cdd:COG2084    82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269 161 GPPGAGQVAKACNQMIMVAAIQACAEAMRLADAHGVDLAAVRTALSGGSAGSRVLEVMGAKMVERDFAAGVEARLHHKDF 240
Cdd:COG2084   162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1003328269 241 ALLMDEAARLGAPLPVAAQVWQQLNALMGAGWGRDDTSSLLRVL 284
Cdd:COG2084   242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-284 2.17e-110

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 320.91  E-value: 2.17e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPLYATPAELAARSEVVITIVTASADVDALAFGPDGL 80
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  81 AAGFAPGAIHVDMSTIAPAMARSLAERHAARGIGFVDAPVSGGGQGARDATLAIMAGAEADVLERVRPLLAAMGKRIVHI 160
Cdd:COG2084    82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269 161 GPPGAGQVAKACNQMIMVAAIQACAEAMRLADAHGVDLAAVRTALSGGSAGSRVLEVMGAKMVERDFAAGVEARLHHKDF 240
Cdd:COG2084   162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1003328269 241 ALLMDEAARLGAPLPVAAQVWQQLNALMGAGWGRDDTSSLLRVL 284
Cdd:COG2084   242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-285 1.61e-84

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 255.75  E-value: 1.61e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPLYATPAELAARSEVVITIVTASADVDALAFGPDGL 80
Cdd:PRK11559    3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  81 AAGFAPGAIHVDMSTIAPAMARSLAERHAARGIGFVDAPVSGGGQGARDATLAIMAGAEADVLERVRPLLAAMGKRIVHI 160
Cdd:PRK11559   83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269 161 GPPGAGQVAKACNQMIMVAAIQACAEAMRLADAHGVDLAAVRTALSGGSAGSRVLEVMGAKMVERDFAAGVEARLHHKDF 240
Cdd:PRK11559  163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1003328269 241 ALLMDEAARLGAPLPVAAQVWQQLNALMGAGWGRDDTSSLLRVLE 285
Cdd:PRK11559  243 ANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYE 287
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 2-285 1.98e-80

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: 245.18  E-value: 1.98e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   2 KVGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPLYATPAELAARSEVVITIVTASADVDALAFGPDGLA 81
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  82 AGFAPGAIHVDMSTIAPAMARSLAERHAARGIGFVDAPVSGGGQGARDATLAIMAGAEADVLERVRPLLAAMGKRIVHIG 161
Cdd:TIGR01505  81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269 162 PPGAGQVAKACNQMIMVAAIQACAEAMRLADAHGVDLAAVRTALSGGSAGSRVLEVMGAKMVERDFAAGVEARLHHKDFA 241
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1003328269 242 LLMDEAARLGAPLPVAAQVWQQLNALMGAGWGRDDTSSLLRVLE 285
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALE 284
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 2-161 1.41e-57

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: 181.90  E-value: 1.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   2 KVGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPLYATPAELAARSEVVITIVTASADVDALAFGpDGLA 81
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFG-EGLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  82 AGFAPGAIHVDMSTIAPAMARSLAERHAARGIGFVDAPVSGGGQGARDATLAIMAGAEADVLERVRPLLAAMGKRIVHIG 161
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
 3-152 4.47e-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: 40.77  E-value: 4.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   3 VGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPlyatpaelAARSEVVITIVTASADVDALAFGPDGlaa 82
Cdd:cd05266     1 VLILGCGYLGQRLARQLLAQGWQVTGTTRSPEKLAADRPAGVT--------PLAADLTQPGLLADVDHLVISLPPPA--- 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1003328269  83 gfapGAIHVDMSTIAPAMARSLAERHAARGIGFVDAP-VSGGGQGARDATLAimagAEADVLERVRPLLAA 152
Cdd:cd05266    70 ----GSYRGGYDPGLRALLDALAQLPAVQRVIYLSSTgVYGDQQGEWVDETS----PPNPSTESGRALLEA 132
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-284 2.17e-110

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 320.91  E-value: 2.17e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPLYATPAELAARSEVVITIVTASADVDALAFGPDGL 80
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  81 AAGFAPGAIHVDMSTIAPAMARSLAERHAARGIGFVDAPVSGGGQGARDATLAIMAGAEADVLERVRPLLAAMGKRIVHI 160
Cdd:COG2084    82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269 161 GPPGAGQVAKACNQMIMVAAIQACAEAMRLADAHGVDLAAVRTALSGGSAGSRVLEVMGAKMVERDFAAGVEARLHHKDF 240
Cdd:COG2084   162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1003328269 241 ALLMDEAARLGAPLPVAAQVWQQLNALMGAGWGRDDTSSLLRVL 284
Cdd:COG2084   242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-285 1.61e-84

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 255.75  E-value: 1.61e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPLYATPAELAARSEVVITIVTASADVDALAFGPDGL 80
Cdd:PRK11559    3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  81 AAGFAPGAIHVDMSTIAPAMARSLAERHAARGIGFVDAPVSGGGQGARDATLAIMAGAEADVLERVRPLLAAMGKRIVHI 160
Cdd:PRK11559   83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269 161 GPPGAGQVAKACNQMIMVAAIQACAEAMRLADAHGVDLAAVRTALSGGSAGSRVLEVMGAKMVERDFAAGVEARLHHKDF 240
Cdd:PRK11559  163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1003328269 241 ALLMDEAARLGAPLPVAAQVWQQLNALMGAGWGRDDTSSLLRVLE 285
Cdd:PRK11559  243 ANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYE 287
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 2-285 1.98e-80

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: 245.18  E-value: 1.98e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   2 KVGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPLYATPAELAARSEVVITIVTASADVDALAFGPDGLA 81
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  82 AGFAPGAIHVDMSTIAPAMARSLAERHAARGIGFVDAPVSGGGQGARDATLAIMAGAEADVLERVRPLLAAMGKRIVHIG 161
Cdd:TIGR01505  81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269 162 PPGAGQVAKACNQMIMVAAIQACAEAMRLADAHGVDLAAVRTALSGGSAGSRVLEVMGAKMVERDFAAGVEARLHHKDFA 241
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1003328269 242 LLMDEAARLGAPLPVAAQVWQQLNALMGAGWGRDDTSSLLRVLE 285
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALE 284
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
1-285 7.16e-60

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 192.54  E-value: 7.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRAAGHDLAVWARRPAsAAALVAEGVPLYATPAELAARSEVVITIVTASADVDALAFGPDGL 80
Cdd:PRK15059    1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGPV-ADELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  81 AAGFAPGAIHVDMSTIAPAMARSLAERHAARGIGFVDAPVSGGGQGARDATLAIMAGAEADVLERVRPLLAAMGKRIVHI 160
Cdd:PRK15059   80 TKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269 161 GPPGAGQVAKACNQMIMVAAIQACAEAMRLADAHGVDLAAVRTALSGGSAGSRVLEVMGAKMVERDFAAGVEARLHHKDF 240
Cdd:PRK15059  160 GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1003328269 241 ALLMDEAARLGAPLPVAAQVWQQLNALMGAGWGRDDTSSLLRVLE 285
Cdd:PRK15059  240 NLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALE 284
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 2-161 1.41e-57

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: 181.90  E-value: 1.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   2 KVGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPLYATPAELAARSEVVITIVTASADVDALAFGpDGLA 81
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFG-EGLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  82 AGFAPGAIHVDMSTIAPAMARSLAERHAARGIGFVDAPVSGGGQGARDATLAIMAGAEADVLERVRPLLAAMGKRIVHIG 161
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 5-284 4.14e-55

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: 179.99  E-value: 4.14e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   5 FIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPLYATPAELAARSEVVITIVTASADVDALAFGPDGLAAGF 84
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  85 APGAIHVDMSTIAPAMARSLAERHAARGIGFVDAPVSGGGQGARDATLAIMAGAEADVLERVRPLLAAMGKRIVHIGPPG 164
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269 165 AGQVAKACNQMIMVAAIQACAEAMRLADAHGVDLAAVRTALSGGSAGSRVLE-------VMGAKMVERDFAAGVEARLHH 237
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDtynpvpgVMPQAPASNGYQGGFGTALML 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1003328269 238 KDFALLMDEAARLGAPLPVAAQVWQQLNALMGAGWGRDDTSSLLRVL 284
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
2-288 3.25e-46

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 157.33  E-value: 3.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   2 KVGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPLYATPAELAARSEVVITIVTASADVDALAFGPDGLA 81
Cdd:PRK15461    3 AIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  82 AGFAPGAIHVDMSTIAPAMARSLAERHAARGIGFVDAPVSGGGQGARDATLAIMAGAEADVLERVRPLLAAMGKRIVHIG 161
Cdd:PRK15461   83 EGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269 162 PPGAGQVAKACNQMIMVAAIQACAEAMRLADAHGVDLAAVRTALSGGSAG-SRVLEVMGAKMVERDFAAGVEARLHHKDF 240
Cdd:PRK15461  163 GPGMGIRVKLINNYMSIALNALSAEAAVLCEALGLSFDVALKVMSGTAAGkGHFTTTWPNKVLKGDLSPAFMIDLAHKDL 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1003328269 241 ALLMDEAARLGAPLPVAAQVWQQLNALMGAGWGRDDTSSLLRVLEAAS 288
Cdd:PRK15461  243 GIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSA 290
PLN02858 PLN02858
fructose-bisphosphate aldolase
 2-285 2.09e-32

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 126.50  E-value: 2.09e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269    2 KVGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPLYATPAELAARSEVVITIVTASADVDALAFGPDGLA 81
Cdd:PLN02858   326 RIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAV 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   82 AGFAPGAIHVDMSTIAPAMARSLAERHAA--RGIGFVDAPVSGGGQGARDATLAIMAGAEADVLERVRPLLAAMGKRIVH 159
Cdd:PLN02858   406 SALPAGASIVLSSTVSPGFVIQLERRLENegRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKLYV 485

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  160 I-GPPGAGQVAKACNQMIMVAAIQACAEAMRLADAHGVDLAAVRTALSGGSAGSRVLEVMGAKMVERDFAAGVEARLHHK 238
Cdd:PLN02858   486 IkGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALDIFVK 565

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1003328269  239 DFALLMDEAARLGAPLPVAAQVWQQLNALMGAGWGRDDTSSLLRVLE 285
Cdd:PLN02858   566 DLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVYE 612
PLN02858 PLN02858
fructose-bisphosphate aldolase
 2-286 8.73e-31

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 121.88  E-value: 8.73e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269    2 KVGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPLYATPAELAARSEVVITIVTASADVDALAFGPDGLA 81
Cdd:PLN02858     6 VVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFGDEGAA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   82 AGFAPGAIHVDMSTIAPAMARSLAERHAARG--IGFVDAPVSGGGQGARDATLAIMAGAEADVLERVRPLLAAMGKRIVH 159
Cdd:PLN02858    86 KGLQKGAVILIRSTILPLQLQKLEKKLTERKeqIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKLYT 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  160 I-GPPGAGQVAKACNQMIMVAAIQACAEAMRLADAHGVDLAAVRTALSGGSAGSRVLEVMGAKMVERDFAAGVEARLHHK 238
Cdd:PLN02858   166 FeGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRFLNVLVQ 245

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1003328269  239 DFALLMDEAARLGAPLPVAAQVWQQLNALMGAGWGRDDTSSLLRVLEA 286
Cdd:PLN02858   246 NLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKVWEK 293
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 164-284 7.61e-27

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: 101.45  E-value: 7.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269 164 GAGQVAKACNQMIMVAAIQACAEAMRLADAHGVDLAAVRTALSGGSAGSRVLE-VMGAKMVERDFAAGVEARLHHKDFAL 242
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALEnKFPQRVLSRDFDPGFALDLMLKDLGL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1003328269 243 LMDEAARLGAPLPVAAQVWQQLNALMGAGWGRDDTSSLLRVL 284
Cdd:pfam14833  81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
YqeC COG1023
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
1-209 3.46e-23

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


Pssm-ID: 440646 [Multi-domain]  Cd Length: 300  Bit Score: 96.31  E-value: 3.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPLYATPAELAARSE---VVITIVTASADVDALAfgp 77
Cdd:COG1023     1 MQIGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKLPaprVVWLMVPAGEITDQVI--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  78 DGLAAGFAPGAIHVD--MSTIAPAMARslAERHAARGIGFVDAPVSGGGQGARDAtLAIMAGAEADVLERVRPLLAAM-- 153
Cdd:COG1023    78 EELAPLLEPGDIVIDggNSNYKDDIRR--AEELAEKGIHFVDVGTSGGVWGLENG-YCLMIGGDKEAVERLEPIFKALap 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003328269 154 --GKRIVHIGPPGAGQVAKacnqmiMV------AAIQACAEAMRLADAH--GVDLAAVRTALSGGS 209
Cdd:COG1023   155 gaENGYLHCGPVGAGHFVK------MVhngieyGMMQAYAEGFELLEASefDLDLAEVAEVWRRGS 214
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
1-201 7.17e-23

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 95.59  E-value: 7.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPLYATPAELAARSE---VVITIVTASADVDALAfgp 77
Cdd:PRK09599    1 MQLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPaprVVWLMVPAGEITDATI--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  78 DGLAAGFAPGAIHVD--MSTIAPAMARslAERHAARGIGFVDAPVSGGGQGARDAtLAIMAGAEADVLERVRPLLAAMGK 155
Cdd:PRK09599   78 DELAPLLSPGDIVIDggNSYYKDDIRR--AELLAEKGIHFVDVGTSGGVWGLERG-YCLMIGGDKEAVERLEPIFKALAP 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1003328269 156 RI----VHIGPPGAGQVAKacnqmiMV------AAIQACAEAMRLADAHG--VDLAAV 201
Cdd:PRK09599  155 RAedgyLHAGPVGAGHFVK------MVhngieyGMMQAYAEGFELLEASRfdLDLAAV 206
Gnd COG0362
6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate ...
 3-166 1.35e-10

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


Pssm-ID: 440131 [Multi-domain]  Cd Length: 467  Bit Score: 61.63  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   3 VGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEG------VPlYATPAELAA---RSEVVITIVTASADVDAL 73
Cdd:COG0362     5 IGVIGLAVMGRNLALNIADHGFSVAVYNRTAEKTDAFLAEHgkgkniVG-TYSLEEFVAsleRPRKILLMVKAGKPVDAV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  74 AfgpDGLAAGFAPGAIHVD------MSTIApamaRslAERHAARGIGFVDAPVSGGGQGARDATlAIMAGAEADVLERVR 147
Cdd:COG0362    84 I---EQLLPLLEPGDIIIDggnshfTDTIR----R--EKELAEKGIHFIGMGVSGGEEGALHGP-SIMPGGSKEAYELVK 153

                         170       180
                  ....*....|....*....|....*
gi 1003328269 148 PLLAAMGKRI------VHIGPPGAG 166
Cdd:COG0362   154 PILEAIAAKVdgepcvTYIGPDGAG 178
PLN02350 PLN02350
phosphogluconate dehydrogenase (decarboxylating)
 2-187 1.16e-07

phosphogluconate dehydrogenase (decarboxylating)


Pssm-ID: 215200 [Multi-domain]  Cd Length: 493  Bit Score: 52.41  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   2 KVGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVA----EG-VPLYAT--PAELA---ARSEVVITIVTASADVD 71
Cdd:PLN02350    8 RIGLAGLAVMGQNLALNIAEKGFPISVYNRTTSKVDETVErakkEGnLPLYGFkdPEDFVlsiQKPRSVIILVKAGAPVD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  72 ALAfgpDGLAAGFAPGAIHVDMSTIAPAMARSLAERHAARGIGFVDAPVSGGGQGARDATlAIMAGAEADVLERVRPLL- 150
Cdd:PLN02350   88 QTI---KALSEYMEPGDCIIDGGNEWYENTERRIKEAAEKGLLYLGMGVSGGEEGARNGP-SLMPGGSFEAYKNIEDILe 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1003328269 151 --AAM---GKRIVHIGPPGAGQVAKACNQMIMVAAIQACAEA 187
Cdd:PLN02350  164 kvAAQvddGPCVTYIGPGGAGNFVKMVHNGIEYGDMQLISEA 205
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-61 1.06e-06

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: 48.91  E-value: 1.06e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRAAG---HDLAVWARRPASAAALVAE-GVPLYATPAELAARSEVVI 61
Cdd:COG0345     3 MKIGFIGAGNMGSAIIKGLLKSGvppEDIIVSDRSPERLEALAERyGVRVTTDNAEAAAQADVVV 67
PRK07502 PRK07502
prephenate/arogenate dehydrogenase family protein;
2-157 6.49e-06

prephenate/arogenate dehydrogenase family protein;


Pssm-ID: 236034 [Multi-domain]  Cd Length: 307  Bit Score: 46.89  E-value: 6.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   2 KVGFIGLGVMGEPMARHLRAAG--HDLAVWARRPASAAALVAEGV--PLYATPAELAARSEVVI--TIVTASADVDAlaf 75
Cdd:PRK07502    8 RVALIGIGLIGSSLARAIRRLGlaGEIVGADRSAETRARARELGLgdRVTTSAAEAVKGADLVIlcVPVGASGAVAA--- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  76 gpdGLAAGFAPGAIHVDMSTIAPAMARSLAErHAARGIGFVDA-PVSGGGQGARDATLAIM-----------AGAEADVL 143
Cdd:PRK07502   85 ---EIAPHLKPGAIVTDVGSVKASVIAAMAP-HLPEGVHFIPGhPLAGTEHSGPDAGFAELfenrwciltppEGTDPAAV 160

                         170
                  ....*....|....
gi 1003328269 144 ERVRPLLAAMGKRI 157
Cdd:PRK07502  161 ARLTAFWRALGARV 174
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 1-162 6.58e-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: 46.66  E-value: 6.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRAAGHDLAVWA--RRPASAAALVAEGV--PLYATPAELAARSEVVI--TIVTASADVDALa 74
Cdd:COG0287     2 MRIAIIGLGLIGGSLALALKRAGLAHEVVGvdRSPETLERALELGVidRAATDLEEAVADADLVVlaVPVGATIEVLAE- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  75 fgpdgLAAGFAPGAIHVDM-STIAPAMArsLAERHAARGIGFVDA-PVSG---GGQGARDATL--------AIMAGAEAD 141
Cdd:COG0287    81 -----LAPHLKPGAIVTDVgSVKGAVVE--AAEALLPDGVRFVGGhPMAGtekSGPEAADADLfegapyilTPTEGTDPE 153

                         170       180
                  ....*....|....*....|.
gi 1003328269 142 VLERVRPLLAAMGKRIVHIGP 162
Cdd:COG0287   154 ALERVEELWEALGARVVEMDP 174
PRK09287 PRK09287
NADP-dependent phosphogluconate dehydrogenase;
11-166 1.22e-05

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236453 [Multi-domain]  Cd Length: 459  Bit Score: 46.27  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  11 MGEPMARHLRAAGHDLAVWARRPASAAALVAEG------VPLYaTPAELAARSE---VVITIVTASADVDALAfgpDGLA 81
Cdd:PRK09287    1 MGKNLALNIASHGYTVAVYNRTPEKTDEFLAEEgkgkkiVPAY-TLEEFVASLEkprKILLMVKAGAPVDAVI---EQLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  82 AGFAPGAIHVD------MSTIapamaRSLAErHAARGIGFVDAPVSGGGQGARDATlAIMAGAEADVLERVRPLLAAM-- 153
Cdd:PRK09287   77 PLLEKGDIIIDggnsnyKDTI-----RREKE-LAEKGIHFIGMGVSGGEEGALHGP-SIMPGGQKEAYELVAPILEKIaa 149

                         170
                  ....*....|....*...
gi 1003328269 154 ----GKRIV-HIGPPGAG 166
Cdd:PRK09287  150 kvedGEPCVtYIGPDGAG 167
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-61 1.43e-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: 1.43e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRAAGHDL-AVWARRPASAAALVAE-GVPLYATPAELAARSEVVI 61
Cdd:COG5495     4 MKIGIIGAGRVGTALAAALRAAGHEVvGVYSRSPASAERAAALlGAVPALDLEELAAEADLVL 66
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 1-162 1.10e-04

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 43.44  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   1 MKVGFIG-LGVMGEPMARHLRAAGHDLAVWARRPASAAALVAE-GVPLYATPAELAARSEVVITIVTASADVDALAfgpd 78
Cdd:PRK08655    1 MKISIIGgTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKElGVEYANDNIDAAKDADIVIISVPINVTEDVIK---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  79 GLAAGFAPGAIHVDMSTI----APAMarslaERHAARGIGFVDA-PVSGGGQGARDATLAIMA---GAEADVLERVRPLL 150
Cdd:PRK08655   77 EVAPHVKEGSLLMDVTSVkerpVEAM-----EEYAPEGVEILPThPMFGPRTPSLKGQVVILTpteKRSNPWFDKVKNFL 151

                         170
                  ....*....|..
gi 1003328269 151 AAMGKRIVHIGP 162
Cdd:PRK08655  152 EKEGARVIVTSP 163
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 1-56 1.99e-04

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 42.15  E-value: 1.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPLYATPAELAAR 56
Cdd:PRK06522    1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLRLEDGEITVPVL 56
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
 3-152 4.47e-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: 40.77  E-value: 4.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   3 VGFIGLGVMGEPMARHLRAAGHDLAVWARRPASAAALVAEGVPlyatpaelAARSEVVITIVTASADVDALAFGPDGlaa 82
Cdd:cd05266     1 VLILGCGYLGQRLARQLLAQGWQVTGTTRSPEKLAADRPAGVT--------PLAADLTQPGLLADVDHLVISLPPPA--- 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1003328269  83 gfapGAIHVDMSTIAPAMARSLAERHAARGIGFVDAP-VSGGGQGARDATLAimagAEADVLERVRPLLAA 152
Cdd:cd05266    70 ----GSYRGGYDPGLRALLDALAQLPAVQRVIYLSSTgVYGDQQGEWVDETS----PPNPSTESGRALLEA 132
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
 1-61 5.73e-04

Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy dehydrogenase family; This group contains a variety of proteins variously identified as glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase) and other enzymes of the 2-hydroxyacid dehydrogenase family. GDH catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of 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. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240641 [Multi-domain]  Cd Length: 306  Bit Score: 40.94  E-value: 5.73e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRAAGHDLAVWARRPASaaalvAEGVPLYATPAELA---ARSEVVI 61
Cdd:cd12164   133 RRVGVLGLGELGAAVARRLAALGFPVSGWSRSPKD-----IEGVTCFHGEEGLDaflAQTDILV 191
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-61 1.66e-03

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 39.36  E-value: 1.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRAAG---HDLAVWARRPASAAALVAE-GVPLYATPAELAARSEVVI 61
Cdd:PRK11880    3 KKIGFIGGGNMASAIIGGLLASGvpaKDIIVSDPSPEKRAALAEEyGVRAATDNQEAAQEADVVV 67
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-65 2.37e-03

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 38.75  E-value: 2.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRA-AGHDL-AVWARRPASAAALVAE-GVPLYATPAELAARSEV-VITIVT 65
Cdd:COG0673     4 LRVGIIGAGGIGRAHAPALAAlPGVELvAVADRDPERAEAFAEEyGVRVYTDYEELLADPDIdAVVIAT 72
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
 1-80 2.97e-03

Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; Hydroxy(phenyl)pyruvate reductase (HPPR) catalyzes the NADP-dependent reduction of hydroxyphenylpyruvates, hydroxypyruvate, or pyruvate to its respective lactate. HPPR acts as a dimer and is related to D-isomer-specific 2-hydroxyacid dehydrogenases, a superfamily that includes 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. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240633 [Multi-domain]  Cd Length: 301  Bit Score: 38.60  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRAAGHDLAVWARRPasaaalvAEGVPL--YATPAELAARSEVVITIVTASAD----VDA-- 72
Cdd:cd12156   142 KRVGIVGLGRIGRAIARRLEAFGMEIAYHGRRP-------KPDVPYryYASLLELAAESDVLVVACPGGPAtrhlVNAev 214


                  ....*....
gi 1003328269  73 -LAFGPDGL 80
Cdd:cd12156   215 lEALGPDGV 223
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 1-65 3.61e-03

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 36.80  E-value: 3.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRAAGHDL---AVWARRPASAAALVAE-GVPLYATPAELAARSEV-VITIVT 65
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAelvAILDPNSERAEAVAESfGVEVYSDLEELLNDPEIdAVIVAT 70
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 1-267 8.01e-03

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: 37.14  E-value: 8.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269   1 MKVGFIGLGVMGEPMARHLRAAGHDLAVWArRPASAAALVAEGV-------------PLYATPAELAARSEVVItIVTAS 67
Cdd:COG1893     1 MKIAILGAGAIGGLLGARLARAGHDVTLVA-RGAHAEALRENGLrlespdgdrttvpVPAVTDPEELGPADLVL-VAVKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269  68 ADVDALAfgpDGLAAGFAPGAI----------------HVDMSTIAPAMARSLAERHAA-----RGIGFVDAPVSGGGQG 126
Cdd:COG1893    79 YDLEAAA---EALAPLLGPDTVvlslqnglgheerlaeALGAERVLGGVVTIGATREEPgvvrhTGGGRLVLGELDGGPS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269 127 ARDATLAIM---AGAEADVLERVRPLL---AAMgkrIVHIGPPGAgqVAKACNQMIMVA------AIQACAEAMRLADAH 194
Cdd:COG1893   156 ERLEALAELleaAGIPVEVSDDIRGALwekLLL---NAAINPLTA--LTGAPNGELLADpearalARALMREVLAVARAE 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003328269 195 GVDLAAVRTAlsggsagsRVLEVMGAKMVE------RDFAAG----VEARLHHkdfalLMDEAARLGAPLPVAAQVWQQL 264
Cdd:COG1893   231 GVPLPEDDLE--------ERVAAVAEATADnrssmlQDLEAGrpteIDAINGA-----VVRLARRLGVPTPVNEALYALL 297


                  ...
gi 1003328269 265 NAL 267
Cdd:COG1893   298 KAL 300
 
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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