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Conserved domains on  [gi|688599572|ref|XP_009292434|]
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3-hydroxyisobutyrate dehydrogenase a isoform X2 [Danio rerio]

Protein Classification

HIBADH family dehydrogenase( domain architecture ID 1903435)

HIBADH family dehydrogenase similar to Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase and Pseudomonas aeruginosa NAD-dependent L-serine dehydrogenase

CATH:  1.10.1040.10|3.40.50.720
EC:  1.1.1.-
Gene Ontology:  GO:0030554|GO:0008442|GO:0016616

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
garR super family cl42929
tartronate semialdehyde reductase; Provisional
 37-225 8.96e-100

tartronate semialdehyde reductase; Provisional


The actual alignment was detected with superfamily member TIGR01692:

Pssm-ID: 456274 [Multi-domain]  Cd Length: 288  Bit Score: 291.32  E-value: 8.96e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572   37 FIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNGILRKV 116
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  117 KKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCGHVG 196
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180
                  ....*....|....*....|....*....
gi 688599572  197 SGQAAKICNNMLLAIGMLGTAETMNLGIR 225
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEK 189
 
Name Accession Description Interval E-value
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 37-225 8.96e-100

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: 291.32  E-value: 8.96e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572   37 FIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNGILRKV 116
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  117 KKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCGHVG 196
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180
                  ....*....|....*....|....*....
gi 688599572  197 SGQAAKICNNMLLAIGMLGTAETMNLGIR 225
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEK 189
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 32-226 3.77e-79

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 238.86  E-value: 3.77e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  32 KTPVGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNG 111
Cdd:COG2084    1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572 112 ILRKVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVY 191
Cdd:COG2084   81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 688599572 192 CGHVGSGQAAKICNNMLLAIGMLGTAETMNLGIRQ 226
Cdd:COG2084  161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKA 195
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 35-193 1.50e-61

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: 189.60  E-value: 1.50e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572   35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSnGILR 114
Cdd:pfam03446   2 IGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLLP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688599572  115 KVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCG 193
Cdd:pfam03446  81 GLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
garR PRK11559
tartronate semialdehyde reductase; Provisional
 35-223 5.04e-57

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 182.94  E-value: 5.04e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNGILR 114
Cdd:PRK11559   5 VGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGIIE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572 115 KVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCGH 194
Cdd:PRK11559  85 GAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTGD 164

                        170       180
                 ....*....|....*....|....*....
gi 688599572 195 VGSGQAAKICNNMLLAIGMLGTAETMNLG 223
Cdd:PRK11559 165 IGAGNVTKLANQVIVALNIAAMSEALVLA 193
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 1-126 2.25e-04

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. D-HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. Similar to the structurally distinct L-HicDH, D-HicDH exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. 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.


Pssm-ID: 240620 [Multi-domain]  Cd Length: 323  Bit Score: 41.52  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572   1 MAALFRGYRNFYKRSNKHVELIL-VSCRSMASKTpVGFIGLGNMGTPMARNLLKNGYPVIATDAFPEscKELQDSGAQiL 79
Cdd:cd01619  112 ILALLRNRKYIDERDKNQDLQDAgVIGRELEDQT-VGVVGTGKIGRAVAQRAKGFGMKVIAYDPFRN--PELEDKGVK-Y 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 688599572  80 DSPAEVAEKADrIITM-LPSSPNVIEVYTGSNgiLRKVKKGTLLIDSS 126
Cdd:cd01619  188 VSLEELFKNSD-IISLhVPLTPENHHMINEEA--FKLMKKGVIIINTA 232
 
Name Accession Description Interval E-value
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 37-225 8.96e-100

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: 291.32  E-value: 8.96e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572   37 FIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNGILRKV 116
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  117 KKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCGHVG 196
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180
                  ....*....|....*....|....*....
gi 688599572  197 SGQAAKICNNMLLAIGMLGTAETMNLGIR 225
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEK 189
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 32-226 3.77e-79

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 238.86  E-value: 3.77e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  32 KTPVGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNG 111
Cdd:COG2084    1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572 112 ILRKVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVY 191
Cdd:COG2084   81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 688599572 192 CGHVGSGQAAKICNNMLLAIGMLGTAETMNLGIRQ 226
Cdd:COG2084  161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKA 195
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 35-193 1.50e-61

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: 189.60  E-value: 1.50e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572   35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSnGILR 114
Cdd:pfam03446   2 IGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLLP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688599572  115 KVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCG 193
Cdd:pfam03446  81 GLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
garR PRK11559
tartronate semialdehyde reductase; Provisional
 35-223 5.04e-57

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 182.94  E-value: 5.04e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNGILR 114
Cdd:PRK11559   5 VGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGIIE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572 115 KVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCGH 194
Cdd:PRK11559  85 GAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTGD 164

                        170       180
                 ....*....|....*....|....*....
gi 688599572 195 VGSGQAAKICNNMLLAIGMLGTAETMNLG 223
Cdd:PRK11559 165 IGAGNVTKLANQVIVALNIAAMSEALVLA 193
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 35-220 5.41e-49

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: 161.98  E-value: 5.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572   35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNGILR 114
Cdd:TIGR01505   2 VGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGIIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  115 KVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCGH 194
Cdd:TIGR01505  82 GAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVGG 161

                         170       180
                  ....*....|....*....|....*.
gi 688599572  195 VGSGQAAKICNNMLLAIGMLGTAETM 220
Cdd:TIGR01505 162 NGDGQTCKVANQIIVALNIEAVSEAL 187
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
35-220 3.42e-35

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 126.29  E-value: 3.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPEScKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNGILR 114
Cdd:PRK15059   3 LGFIGLGIMGTPMAINLARAGHQLHVTTIGPVA-DELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGCTK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572 115 KVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCGH 194
Cdd:PRK15059  82 ASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVGG 161

                        170       180
                 ....*....|....*....|....*.
gi 688599572 195 VGSGQAAKICNNMLLAIGMLGTAETM 220
Cdd:PRK15059 162 NGDGQTCKVANQIIVALNIEAVSEAL 187
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
35-222 2.14e-34

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 124.20  E-value: 2.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNGILR 114
Cdd:PRK15461   4 IAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVCE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572 115 KVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCGH 194
Cdd:PRK15461  84 GLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAGG 163

                        170       180
                 ....*....|....*....|....*....
gi 688599572 195 VGSGQAAKICNN-MLLAIGMLgTAETMNL 222
Cdd:PRK15461 164 PGMGIRVKLINNyMSIALNAL-SAEAAVL 191
PLN02858 PLN02858
fructose-bisphosphate aldolase
 29-225 1.86e-27

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 109.94  E-value: 1.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572   29 MASKTPVGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTG 108
Cdd:PLN02858    1 AQSAGVVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  109 SNGILRKVKKGTLLIDSSTIDPA-VSK-EMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMG 186
Cdd:PLN02858   81 DEGAAKGLQKGAVILIRSTILPLqLQKlEKKLTERKEQIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMC 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 688599572  187 ANV-VYCGHVGSGQAAKICNNMLLAIGMLGTAETMNLGIR 225
Cdd:PLN02858  161 QKLyTFEGEIGAGSKVKMVNELLEGIHLVASAEAMALGVR 200
PLN02858 PLN02858
fructose-bisphosphate aldolase
 29-225 2.32e-27

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 109.56  E-value: 2.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572   29 MASKTP--VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVY 106
Cdd:PLN02858  319 MQAKPVkrIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVL 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  107 TGSNGILRKVKKGTLLIDSSTIDPA-VSK-EMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTC 184
Cdd:PLN02858  399 FGDLGAVSALPAGASIVLSSTVSPGfVIQlERRLENEGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSA 478

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 688599572  185 MGANV-VYCGHVGSGQAAKICNNMLLAIGMLGTAETMNLGIR 225
Cdd:PLN02858  479 LSEKLyVIKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGAR 520
YqeC COG1023
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
35-212 6.43e-18

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


Pssm-ID: 440646 [Multi-domain]  Cd Length: 300  Bit Score: 80.52  E-value: 6.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEK--ADRII-TMLPSSP---NVIEvytg 108
Cdd:COG1023    3 IGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKlpAPRVVwLMVPAGEitdQVIE---- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572 109 snGILRKVKKGTLLID---SSTIDpavSKEMAVAAEKMGAVFMDAPVSGGV-----GAAslakltFLVGGVEEEYNAAQE 180
Cdd:COG1023   79 --ELAPLLEPGDIVIDggnSNYKD---DIRRAEELAEKGIHFVDVGTSGGVwglenGYC------LMIGGDKEAVERLEP 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 688599572 181 LLT--CMGAN--VVYCGHVGSGQAAKICNN-----MLLAIG 212
Cdd:COG1023  148 IFKalAPGAEngYLHCGPVGAGHFVKMVHNgieygMMQAYA 188
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
35-212 9.30e-17

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 77.10  E-value: 9.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEK--ADRII-TMLPSSP---NVIEvytg 108
Cdd:PRK09599   3 LGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKlpAPRVVwLMVPAGEitdATID---- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572 109 snGILRKVKKGTLLID---SSTIDpavSKEMAVAAEKMGAVFMDAPVSGGV-----GAAslakltFLVGGVEEEYNAAQE 180
Cdd:PRK09599  79 --ELAPLLSPGDIVIDggnSYYKD---DIRRAELLAEKGIHFVDVGTSGGVwglerGYC------LMIGGDKEAVERLEP 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 688599572 181 LLTCMGANV----VYCGHVGSGQAAKICNN-----MLLAIG 212
Cdd:PRK09599 148 IFKALAPRAedgyLHAGPVGAGHFVKMVHNgieygMMQAYA 188
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 35-93 3.38e-09

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: 55.45  E-value: 3.38e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688599572  35 VGFIGLGNMGTPMARNLLKNGYP---VIATDAFPESCKELQD-SGAQILDSPAEVAEKADRII 93
Cdd:COG0345    5 IGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSPERLEALAErYGVRVTTDNAEAAAQADVVV 67
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 31-93 4.28e-07

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 49.37  E-value: 4.28e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688599572  31 SKTPVGFIGLGNMGTPMARNLLKNGYP---VIATDAFPESCKEL-QDSGAQILDSPAEVAEKADRII 93
Cdd:PRK11880   1 MMKKIGFIGGGNMASAIIGGLLASGVPakdIIVSDPSPEKRAALaEEYGVRAATDNQEAAQEADVVV 67
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 196-225 4.14e-06

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: 44.44  E-value: 4.14e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 688599572  196 GSGQAAKICNNMLLAIGMLGTAETMNLGIR 225
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVK 30
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 35-192 3.90e-05

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: 43.58  E-value: 3.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  35 VGFIGLGNMGTPMARNLLKNGYP--VIATDAFPESCKELQDSGA--QILDSPAEVAEKADRII--TMLPSSPNVIEvytg 108
Cdd:COG0287    4 IAIIGLGLIGGSLALALKRAGLAheVVGVDRSPETLERALELGVidRAATDLEEAVADADLVVlaVPVGATIEVLA---- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572 109 snGILRKVKKGTLLID-SSTIDPAVskEMAVAAEKMGAVFmdapVSG---------GVGAASL-----AK--LTFLVGGV 171
Cdd:COG0287   80 --ELAPHLKPGAIVTDvGSVKGAVV--EAAEALLPDGVRF----VGGhpmagteksGPEAADAdlfegAPyiLTPTEGTD 151

                        170       180
                 ....*....|....*....|.
gi 688599572 172 EEEYNAAQELLTCMGANVVYC 192
Cdd:COG0287  152 PEALERVEELWEALGARVVEM 172
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 35-206 9.70e-05

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 42.85  E-value: 9.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  35 VGFIGLGNMGTPMARNLLKNGYPVIA-------TDAFPESCKE--LQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEV 105
Cdd:PTZ00142   4 IGLIGLAVMGQNLALNIASRGFKISVynrtyekTEEFVKKAKEgnTRVKGYHTLEELVNSLKKPRKVILLIKAGEAVDET 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572 106 YtgsNGILRKVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKlTFLVGGVEEEYNAAQELLTCM 185
Cdd:PTZ00142  84 I---DNLLPLLEKGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGP-SLMPGGNKEAYDHVKDILEKC 159

                        170       180
                 ....*....|....*....|....*..
gi 688599572 186 GANV------VYCGHVGSGQAAKICNN 206
Cdd:PTZ00142 160 SAKVgdspcvTYVGPGSSGHYVKMVHN 186
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 35-104 1.71e-04

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 41.48  E-value: 1.71e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688599572  35 VGFIGLGNMGTPMARNLLKNGYPV-----IATDAFPESCKELQDSGAQILDSPAEVAEKADRIItmLPSSPNVIE 104
Cdd:PLN02688   3 VGFIGAGKMAEAIARGLVASGVVPpsrisTADDSNPARRDVFQSLGVKTAASNTEVVKSSDVII--LAVKPQVVK 75
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 1-126 2.25e-04

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. D-HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. Similar to the structurally distinct L-HicDH, D-HicDH exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. 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.


Pssm-ID: 240620 [Multi-domain]  Cd Length: 323  Bit Score: 41.52  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572   1 MAALFRGYRNFYKRSNKHVELIL-VSCRSMASKTpVGFIGLGNMGTPMARNLLKNGYPVIATDAFPEscKELQDSGAQiL 79
Cdd:cd01619  112 ILALLRNRKYIDERDKNQDLQDAgVIGRELEDQT-VGVVGTGKIGRAVAQRAKGFGMKVIAYDPFRN--PELEDKGVK-Y 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 688599572  80 DSPAEVAEKADrIITM-LPSSPNVIEVYTGSNgiLRKVKKGTLLIDSS 126
Cdd:cd01619  188 VSLEELFKNSD-IISLhVPLTPENHHMINEEA--FKLMKKGVIIINTA 232
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 27-123 3.68e-04

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as 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. Many, not all, members of this family are dimeric.


Pssm-ID: 240649 [Multi-domain]  Cd Length: 306  Bit Score: 40.55  E-value: 3.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  27 RSMASKTpVGFIGLGNMGTPMARNLLKNGYPVIATDAFPEScKELQDSGAQILdSPAEVAEKADRIITMLPSSP---NVI 103
Cdd:cd12172  138 TELYGKT-LGIIGLGRIGKAVARRLSGFGMKVLAYDPYPDE-EFAKEHGVEFV-SLEELLKESDFISLHLPLTPetrHLI 214

                         90       100
                 ....*....|....*....|
gi 688599572 104 evytgSNGILRKVKKGTLLI 123
Cdd:cd12172  215 -----NAAELALMKPGAILI 229
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
36-124 3.70e-04

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 38.37  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572   36 GFIGLGNMGTPMARNLLKNGYP--VIATDAFPESCKELQDS---GAQILDsPAEVAEKADRIITMLPSspnviEVYTGSN 110
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGPHevVVANSRNPEKAEELAEEygvGATAVD-NEEAAEEADVVFLAVKP-----EDAPDVL 74

                          90
                  ....*....|....
gi 688599572  111 GILRKVKKGTLLID 124
Cdd:pfam03807  75 SELSDLLKGKIVIS 88
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 27-123 6.28e-04

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


Pssm-ID: 427007 [Multi-domain]  Cd Length: 178  Bit Score: 39.40  E-value: 6.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572   27 RSMASKTpVGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQiLDSPAEVAEKADRIITMLPSSP---NVI 103
Cdd:pfam02826  32 RELSGKT-VGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELGAR-YVSLDELLAESDVVSLHLPLTPetrHLI 109

                          90       100
                  ....*....|....*....|
gi 688599572  104 evytgSNGILRKVKKGTLLI 123
Cdd:pfam02826 110 -----NAERLALMKPGAILI 124
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 39-140 8.28e-04

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 39.97  E-value: 8.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  39 GLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDS-GAQILDSPAEVAEKADRIITMLP--SSPNVIEvytgsnGILRK 115
Cdd:PRK08655   8 GTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKElGVEYANDNIDAAKDADIVIISVPinVTEDVIK------EVAPH 81

                         90       100
                 ....*....|....*....|....*
gi 688599572 116 VKKGTLLIDSSTIdpavsKEMAVAA 140
Cdd:PRK08655  82 VKEGSLLMDVTSV-----KERPVEA 101
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
 35-140 1.12e-03

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


Pssm-ID: 240634 [Multi-domain]  Cd Length: 318  Bit Score: 39.19  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSpAEVAEKADRIITMLPSSPNVIEVYTGSNgiLR 114
Cdd:cd12157  147 VGILGMGALGRAIARRLSGFGATLLYYDPHPLDQAEEQALNLRRVEL-DELLESSDFLVLALPLTPDTLHLINAEA--LA 223

                         90       100
                 ....*....|....*....|....*.
gi 688599572 115 KVKKGTLLIDSSTidPAVSKEMAVAA 140
Cdd:cd12157  224 KMKPGALLVNPCR--GSVVDEAAVAE 247
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 38-79 1.79e-03

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


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 38.51  E-value: 1.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 688599572  38 IGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQIL 79
Cdd:COG0569  101 IGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVI 142
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
 30-123 2.84e-03

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: 37.86  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688599572  30 ASKTPVGFIGLGNMGTPMARNLLKNGYPVIATDAFPescKELQD----SGAQILDspaEVAEKADRIITMLPSSPNviev 105
Cdd:cd12164  130 AAERRVGVLGLGELGAAVARRLAALGFPVSGWSRSP---KDIEGvtcfHGEEGLD---AFLAQTDILVCLLPLTPE---- 199

                         90       100
                 ....*....|....*....|...
gi 688599572 106 ytgSNGIL-----RKVKKGTLLI 123
Cdd:cd12164  200 ---TRGILnaellARLPRGAALI 219
 
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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