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Conserved domains on  [gi|1755651452|gb|QEY23483|]
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3-hydroxyisobutyrate dehydrogenase [Neisseria animalis]

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
 8-294 2.18e-124

tartronate semialdehyde reductase; Provisional


The actual alignment was detected with superfamily member TIGR01692:

Pssm-ID: 456274 [Multi-domain]  Cd Length: 288  Bit Score: 356.80  E-value: 2.18e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   8 FVGLGNMGAPMAANLLKKGYALQVSDLNPDAVSALTKQGALYAADLTQAAAQADAVITMLPAGKHVKSVYLGENGLFGRL 87
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  88 KPDTLVIDCSTIAADDARELAAEAQAHRLRFLEAPVSGGISGAAAGTLSFMIGGSGADFQTAKPLLESMGKNIFHAGGSG 167
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452 168 AGQTAKICNNMLLSILMTGTAEALALGIKNGLDPKVLSGIMAASSGGNWVLDRYNPYPGVIPESPASKGYRNGFMSALML 247
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVPGVMPQAPASNGYQGGFGTALML 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1755651452 248 KDLDLALDNARTVGLAAPMGENARALYLNMKARGLLDSDFSAVMKLY 294
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
 
Name Accession Description Interval E-value
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 8-294 2.18e-124

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: 356.80  E-value: 2.18e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   8 FVGLGNMGAPMAANLLKKGYALQVSDLNPDAVSALTKQGALYAADLTQAAAQADAVITMLPAGKHVKSVYLGENGLFGRL 87
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  88 KPDTLVIDCSTIAADDARELAAEAQAHRLRFLEAPVSGGISGAAAGTLSFMIGGSGADFQTAKPLLESMGKNIFHAGGSG 167
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452 168 AGQTAKICNNMLLSILMTGTAEALALGIKNGLDPKVLSGIMAASSGGNWVLDRYNPYPGVIPESPASKGYRNGFMSALML 247
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVPGVMPQAPASNGYQGGFGTALML 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1755651452 248 KDLDLALDNARTVGLAAPMGENARALYLNMKARGLLDSDFSAVMKLY 294
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 5-294 2.39e-113

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 328.61  E-value: 2.39e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   5 NILFVGLGNMGAPMAANLLKKGYALQVSDLNPDAVSALTKQGALYAADLTQAAAQADAVITMLPAGKHVKSVYLGENGLF 84
Cdd:COG2084     3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  85 GRLKPDTLVIDCSTIAADDARELAAEAQAHRLRFLEAPVSGGISGAAAGTLSFMIGGSGADFQTAKPLLESMGKNIFHAG 164
Cdd:COG2084    83 AALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452 165 GSGAGQTAKICNNMLLSILMTGTAEALALGIKNGLDPKVLSGIMAASSGGNWVLDRYNPYpgvipesPASKGYRNGFMSA 244
Cdd:COG2084   163 DAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPR-------MLAGDFDPGFALD 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1755651452 245 LMLKDLDLALDNARTVGLAAPMGENARALYLNMKARGLLDSDFSAVMKLY 294
Cdd:COG2084   236 LMLKDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 4-299 3.00e-69

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 216.84  E-value: 3.00e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   4 QNILFVGLGNMGAPMAANLLKKGYALQVSDLNPDAVSALTKQGALYAADLTQAAAQADAVITMLPAGKHVKSVYLGENGL 83
Cdd:PRK11559    3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  84 FGRLKPDTLVIDCSTIAADDARELAAEAQAHRLRFLEAPVSGGISGAAAGTLSFMIGGSGADFQTAKPLLESMGKNIFHA 163
Cdd:PRK11559   83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452 164 GGSGAGQTAKICNNMLLSILMTGTAEALALGIKNGLDPKVLSGIMAASSGGNWVLDRYNPYpgVIpespaSKGYRNGFMS 243
Cdd:PRK11559  163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPM--VM-----DRNFKPGFRI 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1755651452 244 ALMLKDLDLALDNARTVGLAAPMGENARALYLNMKARGLLDSDFSAVMKLYTDIVK 299
Cdd:PRK11559  236 DLHIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEKLAK 291
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 5-164 2.13e-64

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: 199.62  E-value: 2.13e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   5 NILFVGLGNMGAPMAANLLKKGYALQVSDLNPDAVSALTKQGALYAADLTQAAAQADAVITMLPAGKHVKSVYLGEnGLF 84
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  85 GRLKPDTLVIDCSTIAADDARELAAEAQAHRLRFLEAPVSGGISGAAAGTLSFMIGGSGADFQTAKPLLESMGKNIFHAG 164
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 6-129 1.90e-03

Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related dehydrogenases; The formate/glycerate dehydrogenase like family contains a diverse group of enzymes such as formate dehydrogenase (FDH), glycerate dehydrogenase (GDH), D-lactate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine hydrolase, that share a common 2-domain structure. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar domains of the alpha/beta Rossmann fold NAD+ binding form. The NAD(P) binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD(P) is bound, primarily to the C-terminal portion of the 2nd (internal) domain. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. 2-hydroxyacid dehydrogenases are enzymes that 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 dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of a hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases.


Pssm-ID: 240631 [Multi-domain]  Cd Length: 310  Bit Score: 39.14  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   6 ILFVGLGNMGAPMAANLLKKGYALQVSDLNPDAVSALTKQGALYAADLTQAAAQADAVITMLPAGKHVKSVYLGENgLFG 85
Cdd:cd12154   163 VVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGGKNVEELEEALAEADVIVTTTLLPGKRAGILVPEE-LVE 241

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1755651452  86 RLKPDTLVIDCstiaaddARELAAEAQAHRLRFLEAPVSGGISG 129
Cdd:cd12154   242 QMKPGSVIVNV-------AVGAVGCVQALHTQLLEEGHGVVHYG 278
 
Name Accession Description Interval E-value
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 8-294 2.18e-124

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: 356.80  E-value: 2.18e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   8 FVGLGNMGAPMAANLLKKGYALQVSDLNPDAVSALTKQGALYAADLTQAAAQADAVITMLPAGKHVKSVYLGENGLFGRL 87
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  88 KPDTLVIDCSTIAADDARELAAEAQAHRLRFLEAPVSGGISGAAAGTLSFMIGGSGADFQTAKPLLESMGKNIFHAGGSG 167
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452 168 AGQTAKICNNMLLSILMTGTAEALALGIKNGLDPKVLSGIMAASSGGNWVLDRYNPYPGVIPESPASKGYRNGFMSALML 247
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVPGVMPQAPASNGYQGGFGTALML 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1755651452 248 KDLDLALDNARTVGLAAPMGENARALYLNMKARGLLDSDFSAVMKLY 294
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 5-294 2.39e-113

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 328.61  E-value: 2.39e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   5 NILFVGLGNMGAPMAANLLKKGYALQVSDLNPDAVSALTKQGALYAADLTQAAAQADAVITMLPAGKHVKSVYLGENGLF 84
Cdd:COG2084     3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  85 GRLKPDTLVIDCSTIAADDARELAAEAQAHRLRFLEAPVSGGISGAAAGTLSFMIGGSGADFQTAKPLLESMGKNIFHAG 164
Cdd:COG2084    83 AALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452 165 GSGAGQTAKICNNMLLSILMTGTAEALALGIKNGLDPKVLSGIMAASSGGNWVLDRYNPYpgvipesPASKGYRNGFMSA 244
Cdd:COG2084   163 DAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPR-------MLAGDFDPGFALD 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1755651452 245 LMLKDLDLALDNARTVGLAAPMGENARALYLNMKARGLLDSDFSAVMKLY 294
Cdd:COG2084   236 LMLKDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 4-299 3.00e-69

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 216.84  E-value: 3.00e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   4 QNILFVGLGNMGAPMAANLLKKGYALQVSDLNPDAVSALTKQGALYAADLTQAAAQADAVITMLPAGKHVKSVYLGENGL 83
Cdd:PRK11559    3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  84 FGRLKPDTLVIDCSTIAADDARELAAEAQAHRLRFLEAPVSGGISGAAAGTLSFMIGGSGADFQTAKPLLESMGKNIFHA 163
Cdd:PRK11559   83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452 164 GGSGAGQTAKICNNMLLSILMTGTAEALALGIKNGLDPKVLSGIMAASSGGNWVLDRYNPYpgVIpespaSKGYRNGFMS 243
Cdd:PRK11559  163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPM--VM-----DRNFKPGFRI 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1755651452 244 ALMLKDLDLALDNARTVGLAAPMGENARALYLNMKARGLLDSDFSAVMKLYTDIVK 299
Cdd:PRK11559  236 DLHIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEKLAK 291
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 5-164 2.13e-64

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: 199.62  E-value: 2.13e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   5 NILFVGLGNMGAPMAANLLKKGYALQVSDLNPDAVSALTKQGALYAADLTQAAAQADAVITMLPAGKHVKSVYLGEnGLF 84
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  85 GRLKPDTLVIDCSTIAADDARELAAEAQAHRLRFLEAPVSGGISGAAAGTLSFMIGGSGADFQTAKPLLESMGKNIFHAG 164
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
6-291 1.32e-56

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 184.29  E-value: 1.32e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   6 ILFVGLGNMGAPMAANLLKKGYALQVSDLNPDAVSALTKQGALYAADLTQAAAQADAVITMLPAGKHVKSVYLGENGLFG 85
Cdd:PRK15461    4 IAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVCE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  86 RLKPDTLVIDCSTIAADDARELAAEAQAHRLRFLEAPVSGGISGAAAGTLSFMIGGSGADFQTAKPLLESMGKNIFHAGG 165
Cdd:PRK15461   84 GLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAGG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452 166 SGAGQTAKICNNMLLSILMTGTAEALALGIKNGLDPKVLSGIMAASSGGNWVLDryNPYPGVIPESPASKgyrnGFMSAL 245
Cdd:PRK15461  164 PGMGIRVKLINNYMSIALNALSAEAAVLCEALGLSFDVALKVMSGTAAGKGHFT--TTWPNKVLKGDLSP----AFMIDL 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1755651452 246 MLKDLDLALDNARTVGLAAPMGENARALYLNMKARGLLDSDFSAVM 291
Cdd:PRK15461  238 AHKDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAIL 283
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
8-292 2.08e-44

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 152.87  E-value: 2.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   8 FVGLGNMGAPMAANLLKKGYALQVSDLNPDAvSALTKQGALYAADLTQAAAQADAVITMLPAGKHVKSVYLGENGLFGRL 87
Cdd:PRK15059    5 FIGLGIMGTPMAINLARAGHQLHVTTIGPVA-DELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGCTKAS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  88 KPDTLVIDCSTIAADDARELAAEAQAHRLRFLEAPVSGGISGAAAGTLSFMIGGSGADFQTAKPLLESMGKNIFHAGGSG 167
Cdd:PRK15059   84 LKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVGGNG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452 168 AGQTAKICNNMLLSILMTGTAEALALGIKNGLDPKVLSGIMAASSGGNWVLDrynpypgVIPESPASKGYRNGFMSALML 247
Cdd:PRK15059  164 DGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILE-------VHGERMIKRTFNPGFKIALHQ 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1755651452 248 KDLDLALDNARTVGLAAPMGENARALYLNMKARGLLDSDFSAVMK 292
Cdd:PRK15059  237 KDLNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQ 281
PLN02858 PLN02858
fructose-bisphosphate aldolase
 2-294 2.30e-32

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 126.50  E-value: 2.30e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452    2 SIQNILFVGLGNMGAPMAANLLKKGYALQVSDLNPDAVSALTKQGALYAADLTQAAAQADAVITMLPAGKHVKSVYLGEN 81
Cdd:PLN02858   323 PVKRIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDL 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   82 GLFGRLKPDTLVIDCSTIAADDARELAA--EAQAHRLRFLEAPVSGGISGAAAGTLSFMIGGSGADFQTAKPLLESMGKN 159
Cdd:PLN02858   403 GAVSALPAGASIVLSSTVSPGFVIQLERrlENEGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEK 482

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  160 I-FHAGGSGAGQTAKICNNMLLSILMTGTAEALALGIKNGLDPKVLSGIMAASSGGNWVL-DR--------YNPYPGVip 229
Cdd:PLN02858   483 LyVIKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFeNRvphmldndYTPYSAL-- 560

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755651452  230 espaskgyrngfmsALMLKDLDLALDNARTVGLAAPMGENARALYLNMKARGLLDSDFSAVMKLY 294
Cdd:PLN02858   561 --------------DIFVKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVY 611
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 167-294 3.77e-32

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: 115.32  E-value: 3.77e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452 167 GAGQTAKICNNMLLSILMTGTAEALALGIKNGLDPKVLSGIMAASSGGNWVLDRYnpypgvIPESPASKGYRNGFMSALM 246
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENK------FPQRVLSRDFDPGFALDLM 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1755651452 247 LKDLDLALDNARTVGLAAPMGENARALYLNMKARGLLDSDFSAVMKLY 294
Cdd:pfam14833  75 LKDLGLALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
PLN02858 PLN02858
fructose-bisphosphate aldolase
 8-294 2.82e-30

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 120.34  E-value: 2.82e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452    8 FVGLGNMGAPMAANLLKKGYALQVSDLNPDAVSALTKQGALYAADLTQAAAQADAVITMLPAGKHVKSVYLGENGLFGRL 87
Cdd:PLN02858     9 FVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFGDEGAAKGL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   88 KPDTLVIDCSTIAADDARELAAEAQAHR--LRFLEAPVSGGISGAAAGTLSFMIGGSGADFQTAKPLLESMGKNIFHA-G 164
Cdd:PLN02858    89 QKGAVILIRSTILPLQLQKLEKKLTERKeqIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKLYTFeG 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  165 GSGAGQTAKICNNMLLSILMTGTAEALALGIKNGLDPKVLSGIMAASSGGNWVLdrYNPYPGVIPESPASKGYRNGFMsa 244
Cdd:PLN02858   169 EIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIF--KNHVPLLLKDDYIEGRFLNVLV-- 244

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1755651452  245 lmlKDLDLALDNARTVGLAAPMGENARALYLNMKARGLLDSDFSAVMKLY 294
Cdd:PLN02858   245 ---QNLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKVW 291
YqeC COG1023
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
6-173 2.35e-26

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


Pssm-ID: 440646 [Multi-domain]  Cd Length: 300  Bit Score: 105.17  E-value: 2.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   6 ILFVGLGNMGAPMAANLLKKGYALQVSDLNPDAVSALTKQGALYAADLTQAAAQADA---VITMLPAGKHVKSVyLGEng 82
Cdd:COG1023     3 IGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKLPAprvVWLMVPAGEITDQV-IEE-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  83 LFGRLKPDTLVIDCS-TIAADDAReLAAEAQAHRLRFLEAPVSGGISGAAAGtLSFMIGGSGADFQTAKPLLESM----G 157
Cdd:COG1023    80 LAPLLEPGDIVIDGGnSNYKDDIR-RAEELAEKGIHFVDVGTSGGVWGLENG-YCLMIGGDKEAVERLEPIFKALapgaE 157

                         170
                  ....*....|....*.
gi 1755651452 158 KNIFHAGGSGAGQTAK 173
Cdd:COG1023   158 NGYLHCGPVGAGHFVK 173
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
6-173 3.76e-26

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 104.45  E-value: 3.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   6 ILFVGLGNMGAPMAANLLKKGYALQVSDLNPDAVSALTKQGALYAADLTQAAAQADA---VITMLPAGKHVKSVyLGEng 82
Cdd:PRK09599    3 LGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPAprvVWLMVPAGEITDAT-IDE-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  83 LFGRLKPDTLVID-CSTIAADDARElAAEAQAHRLRFLEAPVSGGISGAAAGtLSFMIGGSGADFQTAKPLLESM---GK 158
Cdd:PRK09599   80 LAPLLSPGDIVIDgGNSYYKDDIRR-AELLAEKGIHFVDVGTSGGVWGLERG-YCLMIGGDKEAVERLEPIFKALaprAE 157

                         170
                  ....*....|....*.
gi 1755651452 159 NIF-HAGGSGAGQTAK 173
Cdd:PRK09599  158 DGYlHAGPVGAGHFVK 173
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 4-101 3.55e-08

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 53.53  E-value: 3.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   4 QNILFVGLGNMGAPMAANLLKKGYA---LQVSDLNPDAVSALTKQ-GALYAADLTQAAAQADAVI-TMLPagKHVKSVyL 78
Cdd:COG0345     3 MKIGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSPERLEALAERyGVRVTTDNAEAAAQADVVVlAVKP--QDLAEV-L 79

                          90       100
                  ....*....|....*....|...
gi 1755651452  79 GEngLFGRLKPDTLVIdcsTIAA 101
Cdd:COG0345    80 EE--LAPLLDPDKLVI---SIAA 97
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 5-64 1.08e-05

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 45.91  E-value: 1.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755651452   5 NILFVGLGNMGAPMAANLLKKGYA---LQVSDLNPDAVSALTKQ-GALYAADLTQAAAQADAVI 64
Cdd:PRK11880    4 KIGFIGGGNMASAIIGGLLASGVPakdIIVSDPSPEKRAALAEEyGVRAATDNQEAAQEADVVV 67
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 3-119 2.61e-05

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 45.15  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   3 IQNILFVGLGNMGAPMAANLLKKGYALQVSDLNPDAV--------SALTKQGAL-----------YAADLTQAAAQADAV 63
Cdd:PRK06130    4 IQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALerargvieRALGVYAPLgiasagmgrirMEAGLAAAVSGADLV 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  64 ITMLPAGKHVKSvylgenGLFGRLkpDTLvIDCSTIAADDARELA----AEAQAHRLRFL 119
Cdd:PRK06130   84 IEAVPEKLELKR------DVFARL--DGL-CDPDTIFATNTSGLPitaiAQAVTRPERFV 134
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 3-110 2.62e-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: 44.73  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   3 IQNILFVGLGNMGAPMAANLLKKGYALQVS--DLNPDAVSALTKQGAL--YAADLTQAAAQADAVI------TMLPAGKH 72
Cdd:COG0287     1 FMRIAIIGLGLIGGSLALALKRAGLAHEVVgvDRSPETLERALELGVIdrAATDLEEAVADADLVVlavpvgATIEVLAE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1755651452  73 VKSvylgenglfgRLKPDTLVID-CSTIAA--DDARELAAE 110
Cdd:COG0287    81 LAP----------HLKPGAIVTDvGSVKGAvvEAAEALLPD 111
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 5-221 7.30e-05

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 44.01  E-value: 7.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   5 NILFVGLGNMGAPMAANLLKKGYALQVSDLNPDAVSALTK---------QGALYAADLTQAAAQADAVITMLPAGKHVKS 75
Cdd:PTZ00142    3 DIGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEEFVKkakegntrvKGYHTLEELVNSLKKPRKVILLIKAGEAVDE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  76 VYlgeNGLFGRLKPDTLVIDCSTIAADDARELAAEAQAHRLRFLEAPVSGGISGAAAGTlSFMIGGSGADFQTAKPLLES 155
Cdd:PTZ00142   83 TI---DNLLPLLEKGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGP-SLMPGGNKEAYDHVKDILEK 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755651452 156 MGKNI------FHAGGSGAGQTAKICNNMLLSILMTGTAEALALgIK--NGLDPKVLSGIMAASSGGNwvLDRY 221
Cdd:PTZ00142  159 CSAKVgdspcvTYVGPGSSGHYVKMVHNGIEYGDMQLISESYKL-MKhiLGMSNEELSEVFNKWNEGI--LNSY 229
PRK09287 PRK09287
NADP-dependent phosphogluconate dehydrogenase;
14-156 8.09e-05

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236453 [Multi-domain]  Cd Length: 459  Bit Score: 43.96  E-value: 8.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  14 MGAPMAANLLKKGYALQVSDLNPDAVSALTKQ----GALYAA----DLTQAAAQADAVITMLPAGKHVKSVYlgeNGLFG 85
Cdd:PRK09287    1 MGKNLALNIASHGYTVAVYNRTPEKTDEFLAEegkgKKIVPAytleEFVASLEKPRKILLMVKAGAPVDAVI---EQLLP 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755651452  86 RLKPDTLVIDC------STIAaddaRElaAEAQAHRLRFLEAPVSGGISGAAAGTlSFMIGGSGADFQTAKPLLESM 156
Cdd:PRK09287   78 LLEKGDIIIDGgnsnykDTIR----RE--KELAEKGIHFIGMGVSGGEEGALHGP-SIMPGGQKEAYELVAPILEKI 147
MviM COG0673
Predicted dehydrogenase [General function prediction only];
5-121 7.62e-04

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 40.29  E-value: 7.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   5 NILFVGLGNMGAPMAANLLK-KGYALQ-VSDLNPDAVSALTKQ-GALYAADLTQAAAQA--DAV-------------ITM 66
Cdd:COG0673     5 RVGIIGAGGIGRAHAPALAAlPGVELVaVADRDPERAEAFAEEyGVRVYTDYEELLADPdiDAVviatpnhlhaelaIAA 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1755651452  67 LPAGKHVksvyLGEnglfgrlKPdtLVIDcstiaADDARELAAEAQAHRLRFLEA 121
Cdd:COG0673    85 LEAGKHV----LCE-------KP--LALT-----LEEARELVAAAEEAGVVLMVG 121
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
 9-156 1.19e-03

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 40.11  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   9 VGLGNMGApMAANLLKKGYALQVSDLNPdAVSALTKQGALYAADLTQAAAQADAVITMLPAGKHvkSVYLGENGLFGRLK 88
Cdd:PRK08605  152 IGTGRIGL-AVAKIFAKGYGSDVVAYDP-FPNAKAATYVDYKDTIEEAVEGADIVTLHMPATKY--NHYLFNADLFKHFK 227

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755651452  89 PDTLVIDCSTIAADDARELaaeaqahrlrfLEAPVSGGISGAAAGTLSFMIGGSGADFQTAK---PLLESM 156
Cdd:PRK08605  228 KGAVFVNCARGSLVDTKAL-----------LDALDNGLIKGAALDTYEFERPLFPSDQRGQTindPLLESL 287
PLN02350 PLN02350
phosphogluconate dehydrogenase (decarboxylating)
 6-177 1.58e-03

phosphogluconate dehydrogenase (decarboxylating)


Pssm-ID: 215200 [Multi-domain]  Cd Length: 493  Bit Score: 39.70  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   6 ILFVGLGNMGAPMAANLLKKGYALQVSDLNPD----AVSALTKQGAL------YAADLTQAAAQADAVITMLPAGKHVKS 75
Cdd:PLN02350    9 IGLAGLAVMGQNLALNIAEKGFPISVYNRTTSkvdeTVERAKKEGNLplygfkDPEDFVLSIQKPRSVIILVKAGAPVDQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452  76 VYlgeNGLFGRLKPDTLVIDCSTIAADDARELAAEAQAHRLRFLEAPVSGGISGAAAGTlSFMIGGSGADFQTAKPLLES 155
Cdd:PLN02350   89 TI---KALSEYMEPGDCIIDGGNEWYENTERRIKEAAEKGLLYLGMGVSGGEEGARNGP-SLMPGGSFEAYKNIEDILEK 164

                         170       180
                  ....*....|....*....|....*...
gi 1755651452 156 M------GKNIFHAGGSGAGQTAKICNN 177
Cdd:PLN02350  165 VaaqvddGPCVTYIGPGGAGNFVKMVHN 192
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 6-129 1.90e-03

Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related dehydrogenases; The formate/glycerate dehydrogenase like family contains a diverse group of enzymes such as formate dehydrogenase (FDH), glycerate dehydrogenase (GDH), D-lactate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine hydrolase, that share a common 2-domain structure. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar domains of the alpha/beta Rossmann fold NAD+ binding form. The NAD(P) binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD(P) is bound, primarily to the C-terminal portion of the 2nd (internal) domain. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. 2-hydroxyacid dehydrogenases are enzymes that 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 dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of a hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases.


Pssm-ID: 240631 [Multi-domain]  Cd Length: 310  Bit Score: 39.14  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   6 ILFVGLGNMGAPMAANLLKKGYALQVSDLNPDAVSALTKQGALYAADLTQAAAQADAVITMLPAGKHVKSVYLGENgLFG 85
Cdd:cd12154   163 VVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGGKNVEELEEALAEADVIVTTTLLPGKRAGILVPEE-LVE 241

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1755651452  86 RLKPDTLVIDCstiaaddARELAAEAQAHRLRFLEAPVSGGISG 129
Cdd:cd12154   242 QMKPGSVIVNV-------AVGAVGCVQALHTQLLEEGHGVVHYG 278
Wzb COG0394
Protein-tyrosine-phosphatase [Signal transduction mechanisms];
1-66 5.91e-03

Protein-tyrosine-phosphatase [Signal transduction mechanisms];


Pssm-ID: 440163  Cd Length: 137  Bit Score: 36.29  E-value: 5.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755651452   1 MSIQNILFVGLGNMG-APMAANLLKKGYALQV----------SDLNPDAVSALTKQG----ALYAADLTQA-AAQADAVI 64
Cdd:COG0394     1 MMPKRVLFVCTGNICrSPMAEALLRHLAGGRVevdsagtepgGPVDPRAVAVLAERGidlsGHRSRQLDEEdLPEFDLVI 80


                  ..
gi 1755651452  65 TM 66
Cdd:COG0394    81 TM 82
 
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.
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