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Conserved domains on  [gi|499999853|ref|WP_011680571|]
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MULTISPECIES: NAD(P)-dependent oxidoreductase [Leuconostoc]

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 ...
 1-283 2.15e-121

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


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 348.64  E-value: 2.15e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   1 MNIGFIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNNGAIWRDTPAKVAQYSDITFTMVGYPKDVEEVWTSEDGV 80
Cdd:COG2084    2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  81 FAGAKEGSILVDMTTSTPRLAEQLAQTGADLGFKVLDAPVSGGDIGAKNGTLAIMVGGEQQVLDEIKPVLSVIGQQIVFA 160
Cdd:COG2084   82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853 161 GSAGKGQHMKMSNNIGVAATVITMAESLVYAKAAGLDLESAYNVWRKGAAGSWSVDNYIPRIFQGDYAPGFYVKHLLKDL 240
Cdd:COG2084  162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 499999853 241 RIALDAAKEMDIDLPNTKLAEQLFERLSQE-HGDEGVQAIVKLW 283
Cdd:COG2084  242 GLALEAARAAGVPLPLAAAARQLYARAVAAgHGDEDFSALIKLL 285
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-283 2.15e-121

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 348.64  E-value: 2.15e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   1 MNIGFIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNNGAIWRDTPAKVAQYSDITFTMVGYPKDVEEVWTSEDGV 80
Cdd:COG2084    2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  81 FAGAKEGSILVDMTTSTPRLAEQLAQTGADLGFKVLDAPVSGGDIGAKNGTLAIMVGGEQQVLDEIKPVLSVIGQQIVFA 160
Cdd:COG2084   82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853 161 GSAGKGQHMKMSNNIGVAATVITMAESLVYAKAAGLDLESAYNVWRKGAAGSWSVDNYIPRIFQGDYAPGFYVKHLLKDL 240
Cdd:COG2084  162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 499999853 241 RIALDAAKEMDIDLPNTKLAEQLFERLSQE-HGDEGVQAIVKLW 283
Cdd:COG2084  242 GLALEAARAAGVPLPLAAAARQLYARAVAAgHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-283 2.02e-72

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 224.55  E-value: 2.02e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   1 MNIGFIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNNGAIWRDTPAKVAQYSDITFTMVGYPKDVEEVWTSEDGV 80
Cdd:PRK11559   3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  81 FAGAKEGSILVDMTTSTPRLAEQLAQTGADLGFKVLDAPVSGGDIGAKNGTLAIMVGGEQQVLDEIKPVLSVIGQQIVFA 160
Cdd:PRK11559  83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853 161 GSAGKGQHMKMSNNIGVAATVITMAESLVYAKAAGLDLESAYNVWRKGAAGSWSVDNYIPRIFQGDYAPGFYVKHLLKDL 240
Cdd:PRK11559 163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 499999853 241 RIALDAAKEMDIDLPNTKLAEQLFERLSQE-HGDEGVQAIVKLW 283
Cdd:PRK11559 243 ANALDTSHGVGAPLPLTAAVMEMMQALKADgLGTADHSALACYY 286
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 3-272 1.44e-70

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: 219.76  E-value: 1.44e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853    3 IGFIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNNGAIWRDTPAKVAQYSDITFTMVGYPKDVEEVWTSEDGVFA 82
Cdd:TIGR01505   2 VGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGIIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   83 GAKEGSILVDMTTSTPRLAEQLAQTGADLGFKVLDAPVSGGDIGAKNGTLAIMVGGEQQVLDEIKPVLSVIGQQIVFAGS 162
Cdd:TIGR01505  82 GAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  163 AGKGQHMKMSNNIGVAATVITMAESLVYAKAAGLDLESAYNVWRKGAAGSWSVDNYIPRIFQGDYAPGFYVKHLLKDLRI 242
Cdd:TIGR01505 162 NGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLNL 241

                         250       260       270
                  ....*....|....*....|....*....|
gi 499999853  243 ALDAAKEMDIDLPNTKLAEQLFERLSQEHG 272
Cdd:TIGR01505 242 ALDSAKAVGANLPNTATVQELFNTLRANGG 271
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 2-161 2.17e-58

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: 183.83  E-value: 2.17e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853    2 NIGFIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNNGAIWRDTPAKVAQYSDITFTMVGYPKDVEEVWTsEDGVF 81
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIF-GEGLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   82 AGAKEGSILVDMTTSTPRLAEQLAQTGADLGFKVLDAPVSGGDIGAKNGTLAIMVGGEQQVLDEIKPVLSVIGQQIVFAG 161
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
 1-31 5.35e-03

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. 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: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 37.66  E-value: 5.35e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 499999853   1 MNIGFIG-TGVMGTGIINNLLQAGYEVSVFNR 31
Cdd:cd05265    1 MKILIIGgTRFIGKALVEELLAAGHDVTVFNR 32
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-283 2.15e-121

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 348.64  E-value: 2.15e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   1 MNIGFIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNNGAIWRDTPAKVAQYSDITFTMVGYPKDVEEVWTSEDGV 80
Cdd:COG2084    2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  81 FAGAKEGSILVDMTTSTPRLAEQLAQTGADLGFKVLDAPVSGGDIGAKNGTLAIMVGGEQQVLDEIKPVLSVIGQQIVFA 160
Cdd:COG2084   82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853 161 GSAGKGQHMKMSNNIGVAATVITMAESLVYAKAAGLDLESAYNVWRKGAAGSWSVDNYIPRIFQGDYAPGFYVKHLLKDL 240
Cdd:COG2084  162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 499999853 241 RIALDAAKEMDIDLPNTKLAEQLFERLSQE-HGDEGVQAIVKLW 283
Cdd:COG2084  242 GLALEAARAAGVPLPLAAAARQLYARAVAAgHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-283 2.02e-72

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 224.55  E-value: 2.02e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   1 MNIGFIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNNGAIWRDTPAKVAQYSDITFTMVGYPKDVEEVWTSEDGV 80
Cdd:PRK11559   3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  81 FAGAKEGSILVDMTTSTPRLAEQLAQTGADLGFKVLDAPVSGGDIGAKNGTLAIMVGGEQQVLDEIKPVLSVIGQQIVFA 160
Cdd:PRK11559  83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853 161 GSAGKGQHMKMSNNIGVAATVITMAESLVYAKAAGLDLESAYNVWRKGAAGSWSVDNYIPRIFQGDYAPGFYVKHLLKDL 240
Cdd:PRK11559 163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 499999853 241 RIALDAAKEMDIDLPNTKLAEQLFERLSQE-HGDEGVQAIVKLW 283
Cdd:PRK11559 243 ANALDTSHGVGAPLPLTAAVMEMMQALKADgLGTADHSALACYY 286
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 3-272 1.44e-70

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: 219.76  E-value: 1.44e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853    3 IGFIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNNGAIWRDTPAKVAQYSDITFTMVGYPKDVEEVWTSEDGVFA 82
Cdd:TIGR01505   2 VGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGIIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   83 GAKEGSILVDMTTSTPRLAEQLAQTGADLGFKVLDAPVSGGDIGAKNGTLAIMVGGEQQVLDEIKPVLSVIGQQIVFAGS 162
Cdd:TIGR01505  82 GAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  163 AGKGQHMKMSNNIGVAATVITMAESLVYAKAAGLDLESAYNVWRKGAAGSWSVDNYIPRIFQGDYAPGFYVKHLLKDLRI 242
Cdd:TIGR01505 162 NGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLNL 241

                         250       260       270
                  ....*....|....*....|....*....|
gi 499999853  243 ALDAAKEMDIDLPNTKLAEQLFERLSQEHG 272
Cdd:TIGR01505 242 ALDSAKAVGANLPNTATVQELFNTLRANGG 271
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 2-161 2.17e-58

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: 183.83  E-value: 2.17e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853    2 NIGFIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNNGAIWRDTPAKVAQYSDITFTMVGYPKDVEEVWTsEDGVF 81
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIF-GEGLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   82 AGAKEGSILVDMTTSTPRLAEQLAQTGADLGFKVLDAPVSGGDIGAKNGTLAIMVGGEQQVLDEIKPVLSVIGQQIVFAG 161
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
1-274 3.40e-58

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 187.92  E-value: 3.40e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   1 MNIGFIGTGVMGTGIINNLLQAGYEVSVfNRTHSKANTVLNNGAIWRDTPAKVAQYSDITFTMVGYPKDVEEVWTSEDGV 80
Cdd:PRK15059   1 MKLGFIGLGIMGTPMAINLARAGHQLHV-TTIGPVADELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  81 FAGAKEGSILVDMTTSTPRLAEQLAQTGADLGFKVLDAPVSGGDIGAKNGTLAIMVGGEQQVLDEIKPVLSVIGQQIVFA 160
Cdd:PRK15059  80 TKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853 161 GSAGKGQHMKMSNNIGVAATVITMAESLVYAKAAGLDLESAYNVWRKGAAGSWSVDNYIPRIFQGDYAPGFYVKHLLKDL 240
Cdd:PRK15059 160 GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDL 239

                        250       260       270
                 ....*....|....*....|....*....|....
gi 499999853 241 RIALDAAKEMDIDLPNTKLAEQLFERLSQEHGDE 274
Cdd:PRK15059 240 NLALQSAKALALNLPNTATCQELFNTCAANGGSQ 273
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 5-282 1.33e-56

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: 183.85  E-value: 1.33e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853    5 FIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNNGAIWRDTPAKVAQYSDITFTMVGYPKDVEEVWTSEDGVFAGA 84
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   85 KEGSILVDMTTSTPRLAEQLAQTGADLGFKVLDAPVSGGDIGAKNGTLAIMVGGEQQVLDEIKPVLSVIGQQIVFAGSAG 164
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  165 KGQHMKMSNNIGVAATVITMAESLVYAKAAGLDLESAYNVWRKGAAGSWSVDNYIPriFQG---------DYAPGFYVKH 235
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNP--VPGvmpqapasnGYQGGFGTAL 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 499999853  236 LLKDLRIALDAAKEMDIDLPNTKLAEQLFERL-SQEHGDEGVQAIVKL 282
Cdd:TIGR01692 239 MLKDLGLAQDAAKSAGAPTPLGALARQLYSLFdDKGHGGKDFSSVIQL 286
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
3-264 7.84e-41

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 143.07  E-value: 7.84e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   3 IGFIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNNGAIWRDTPAKVAQYSDITFTMVGYPKDVEEVWTSEDGVFA 82
Cdd:PRK15461   4 IAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVCE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  83 GAKEGSILVDMTTSTPRLAEQLAQTGADLGFKVLDAPVSGGDIGAKNGTLAIMVGGEQQVLDEIKPVLSVIGQQIVFAGS 162
Cdd:PRK15461  84 GLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAGG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853 163 AGKGQHMKMSNN-IGVAATVITmAESLVYAKAAGLDLESAYNVWRKGAAGSWSVDNYIP-RIFQGDYAPGFYVKHLLKDL 240
Cdd:PRK15461 164 PGMGIRVKLINNyMSIALNALS-AEAAVLCEALGLSFDVALKVMSGTAAGKGHFTTTWPnKVLKGDLSPAFMIDLAHKDL 242

                        250       260
                 ....*....|....*....|....
gi 499999853 241 RIALDAAKEMDIDLPNTKLAEQLF 264
Cdd:PRK15461 243 GIALDVANQLHVPMPLGAASREVY 266
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 164-283 8.40e-38

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: 129.57  E-value: 8.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  164 GKGQHMKMSNNIGVAATVITMAESLVYAKAAGLDLESAYNVWRKGAAGSWSVDNYIP-RIFQGDYAPGFYVKHLLKDLRI 242
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFPqRVLSRDFDPGFALDLMLKDLGL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 499999853  243 ALDAAKEMDIDLPNTKLAEQLFERLSQE-HGDEGVQAIVKLW 283
Cdd:pfam14833  81 ALDLARALGVPLPLTALAAQLYQAAAAQgGGDADHSAIIRLL 122
PLN02858 PLN02858
fructose-bisphosphate aldolase
 3-264 9.49e-38

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 141.91  E-value: 9.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853    3 IGFIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNNGAIWRDTPAKVAQYSDITFTMVGYPKDVEEVWTSEDGVFA 82
Cdd:PLN02858  327 IGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAVS 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   83 GAKEGSILVDMTTSTP----RLAEQLAQTGADLgfKVLDAPVSGGDIGAKNGTLAIMVGGEQQVLDEIKPVLSVIGQQI- 157
Cdd:PLN02858  407 ALPAGASIVLSSTVSPgfviQLERRLENEGRDI--KLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKLy 484

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  158 VFAGSAGKGQHMKMSNNIGVAATVITMAESLVYAKAAGLDLESAYNVWRKGAAGSWSVDNYIPRIFQGDYAPGFYVKHLL 237
Cdd:PLN02858  485 VIKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALDIFV 564

                         250       260
                  ....*....|....*....|....*..
gi 499999853  238 KDLRIALDAAKEMDIDLPNTKLAEQLF 264
Cdd:PLN02858  565 KDLGIVSREGSSRKIPLHLSTVAHQLF 591
PLN02858 PLN02858
fructose-bisphosphate aldolase
 3-283 3.36e-34

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 131.51  E-value: 3.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853    3 IGFIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNNGAIWRDTPAKVAQYSDITFTMVGYPKDVEEVWTSEDGVFA 82
Cdd:PLN02858    7 VGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFGDEGAAK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   83 GAKEGSILVDMTTSTP----RLAEQLAQTGADLgfKVLDAPVSGGDIGAKNGTLAIMVGGEQQVLDEIKPVLSVIGQQIV 158
Cdd:PLN02858   87 GLQKGAVILIRSTILPlqlqKLEKKLTERKEQI--FLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKLY 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  159 FA-GSAGKGQHMKMSNNIGVAATVITMAESLVYAKAAGLDLESAYNVWRKGAAGSWSVDNYIPRIFQGDYAPGFYVKHLL 237
Cdd:PLN02858  165 TFeGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRFLNVLV 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 499999853  238 KDLRIALDAAKEMDIDLPNTKLA-EQLFERLSQEHGDEGVQAIVKLW 283
Cdd:PLN02858  245 QNLGIVLDMAKSLPFPLPLLAVAhQQLISGSSSMQGDDTATSLAKVW 291
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
1-216 1.74e-16

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 77.87  E-value: 1.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   1 MNIGFIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNNGAIWRDTPAK-VAQYSD--ITFTMV--GYPkdVEEVWT 75
Cdd:PRK09599   1 MQLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEElVAKLPAprVVWLMVpaGEI--TDATID 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  76 SEDGVFAgakEGSILVDMTTS----TPRLAEQLAQTGADLgfkvLDAPVSGGDIGAKNGtLAIMVGGEQQVLDEIKPVLS 151
Cdd:PRK09599  79 ELAPLLS---PGDIVIDGGNSyykdDIRRAELLAEKGIHF----VDVGTSGGVWGLERG-YCLMIGGDKEAVERLEPIFK 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499999853 152 VIGQQI----VFAGSAGKGQHMKMSNNiGV-----AAtvitMAE--SLVYAKAAGLDLESAYNVWRKGAA-GSWSVD 216
Cdd:PRK09599 151 ALAPRAedgyLHAGPVGAGHFVKMVHN-GIeygmmQA----YAEgfELLEASRFDLDLAAVAEVWRRGSViRSWLLD 222
Gnd COG0362
6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate ...
 1-153 5.10e-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: 59.70  E-value: 5.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   1 MNIGFIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNNGAiwrdtPAKvaqysditfTMVGYpKDVEEvwtsedgv 80
Cdd:COG0362    3 ADIGVIGLAVMGRNLALNIADHGFSVAVYNRTAEKTDAFLAEHG-----KGK---------NIVGT-YSLEE-------- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  81 F---------------AGA-------------KEGSILVDMTTS----TPRLAEQLAQTGadLGFkvLDAPVSGGDIGAK 128
Cdd:COG0362   60 FvaslerprkillmvkAGKpvdavieqllpllEPGDIIIDGGNShftdTIRREKELAEKG--IHF--IGMGVSGGEEGAL 135

                        170       180
                 ....*....|....*....|....*
gi 499999853 129 NGTlAIMVGGEQQVLDEIKPVLSVI 153
Cdd:COG0362  136 HGP-SIMPGGSKEAYELVKPILEAI 159
PLN02350 PLN02350
phosphogluconate dehydrogenase (decarboxylating)
 3-174 8.93e-10

phosphogluconate dehydrogenase (decarboxylating)


Pssm-ID: 215200 [Multi-domain]  Cd Length: 493  Bit Score: 58.96  E-value: 8.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   3 IGFIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNNGAiwRDTPAKVAQYSD--------------ITFTMVGYPK 68
Cdd:PLN02350   9 IGLAGLAVMGQNLALNIAEKGFPISVYNRTTSKVDETVERAK--KEGNLPLYGFKDpedfvlsiqkprsvIILVKAGAPV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  69 DveevwTSEDGVFAGAKEGSILVD----MTTSTPRLAEQLAQtgadLGFKVLDAPVSGGDIGAKNGTlAIMVGGEQQVLD 144
Cdd:PLN02350  87 D-----QTIKALSEYMEPGDCIIDggneWYENTERRIKEAAE----KGLLYLGMGVSGGEEGARNGP-SLMPGGSFEAYK 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 499999853 145 EIKPVLSVIGQQ------IVFAGSAGKGQHMKMSNN 174
Cdd:PLN02350 157 NIEDILEKVAAQvddgpcVTYIGPGGAGNFVKMVHN 192
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 2-213 7.37e-09

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 55.95  E-value: 7.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   2 NIGFIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNNGAiwrDTPAKVAQYSDITfTMV---GYPKDV-------E 71
Cdd:PTZ00142   3 DIGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEEFVKKAK---EGNTRVKGYHTLE-ELVnslKKPRKVillikagE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  72 EVWTSEDGVFAGAKEGSILVDMTTSTPRLAEQLAQTGADLGFKVLDAPVSGGDIGAKNGTlAIMVGGEQQVLDEIKPVLS 151
Cdd:PTZ00142  79 AVDETIDNLLPLLEKGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGP-SLMPGGNKEAYDHVKDILE 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499999853 152 VIGQQI------VFAGSAGKGQHMKMSNNIGVAATVITMAESLVYAKAAG----LDLESAYNVWRKGAAGSW 213
Cdd:PTZ00142 158 KCSAKVgdspcvTYVGPGSSGHYVKMVHNGIEYGDMQLISESYKLMKHILgmsnEELSEVFNKWNEGILNSY 229
PRK07680 PRK07680
late competence protein ComER; Validated
 1-104 2.83e-08

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 53.82  E-value: 2.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   1 MNIGFIGTGVMGTGIINNLLQAGY----EVSVFNRTHSKANTVLNN--GAIWRDTPAKVAQYSDITFTMVG----YP--K 68
Cdd:PRK07680   1 MNIGFIGTGNMGTILIEAFLESGAvkpsQLTITNRTPAKAYHIKERypGIHVAKTIEEVISQSDLIFICVKpldiYPllQ 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499999853  69 DVEEVWTSEdgvfagakegSILVDMTtsTPRLAEQL 104
Cdd:PRK07680  81 KLAPHLTDE----------HCLVSIT--SPISVEQL 104
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-73 5.26e-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: 46.60  E-value: 5.26e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499999853   1 MNIGFIGTGVMGTGIINNLLQAGY---EVSVFNRTHSKANTVLNN-GAIWRDTPAKVAQYSDITFTMVGyPKDVEEV 73
Cdd:COG0345    3 MKIGFIGAGNMGSAIIKGLLKSGVppeDIIVSDRSPERLEALAERyGVRVTTDNAEAAAQADVVVLAVK-PQDLAEV 78
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-61 2.84e-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: 44.80  E-value: 2.84e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499999853   1 MNIGFIGTGVMGTGIINNLLQAGYEVS-VFNRTHSKANTVLNN-GAIWRDTPAKVAQYSDITF 61
Cdd:COG5495    4 MKIGIIGAGRVGTALAAALRAAGHEVVgVYSRSPASAERAAALlGAVPALDLEELAAEADLVL 66
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 1-94 1.19e-04

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 43.05  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   1 MNIGFIG-TGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNN-GAIWRDTPAKVAQYSDITFTMVgyPKDVEEVWTSEd 78
Cdd:PRK08655   1 MKISIIGgTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKElGVEYANDNIDAAKDADIVIISV--PINVTEDVIKE- 77

                         90
                 ....*....|....*.
gi 499999853  79 gVFAGAKEGSILVDMT 94
Cdd:PRK08655  78 -VAPHVKEGSLLMDVT 92
PRK09287 PRK09287
NADP-dependent phosphogluconate dehydrogenase;
11-153 2.33e-04

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236453 [Multi-domain]  Cd Length: 459  Bit Score: 42.42  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  11 MGTGIINNLLQAGYEVSVFNRTHSKANTVLNNgaiwRDTPAKVAQYSDIT------------FTMV--GYPKD------- 69
Cdd:PRK09287   1 MGKNLALNIASHGYTVAVYNRTPEKTDEFLAE----EGKGKKIVPAYTLEefvaslekprkiLLMVkaGAPVDavieqll 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853  70 --VEEvwtsedgvfagakeGSILVD----MTTSTPRLAEQLAQTGadLGFkvLDAPVSGGDIGAKNGTlAIMVGGEQQVL 143
Cdd:PRK09287  77 plLEK--------------GDIIIDggnsNYKDTIRREKELAEKG--IHF--IGMGVSGGEEGALHGP-SIMPGGQKEAY 137

                        170
                 ....*....|
gi 499999853 144 DEIKPVLSVI 153
Cdd:PRK09287 138 ELVAPILEKI 147
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
3-94 1.23e-03

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


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 39.00  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853   3 IGFIGTGVMGTGIINNLLQAGYEVSVFNRTHSKANTVLNN--GAIWRDTPAKVAQYSDITFTMVGYpKDVEEVwtseDGV 80
Cdd:COG2085    1 IGIIGTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAElgPGARAGTNAEAAAAADVVVLAVPY-EAVPDV----LES 75

                         90
                 ....*....|....
gi 499999853  81 FAGAKEGSILVDMT 94
Cdd:COG2085   76 LGDALAGKIVIDAT 89
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
4-94 1.26e-03

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 37.21  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499999853    4 GFIGTGVMGTGIINNLLQAG-YEVSVFN-RTHSKANTVLNNGAIW--RDTPAKVAQYSDITFTMVGyPKDVEEVWTSEDG 79
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGpHEVVVANsRNPEKAEELAEEYGVGatAVDNEEAAEEADVVFLAVK-PEDAPDVLSELSD 79

                          90
                  ....*....|....*
gi 499999853   80 VFAgakeGSILVDMT 94
Cdd:pfam03807  80 LLK----GKIVISIA 90
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
 1-31 5.35e-03

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. 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: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 37.66  E-value: 5.35e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 499999853   1 MNIGFIG-TGVMGTGIINNLLQAGYEVSVFNR 31
Cdd:cd05265    1 MKILIIGgTRFIGKALVEELLAAGHDVTVFNR 32
 
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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