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Conserved domains on  [gi|500166405|ref|WP_011841021|]
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NAD(P)-dependent oxidoreductase [Cereibacter sphaeroides]

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 ...
 1-286 2.83e-116

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


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 335.55  E-value: 2.83e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   1 MAKLAFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAAQhGGRAAATPAEAAEGAAFVMACVGNDDDLRSICRGES 80
Cdd:COG2084    1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAA-GARVAASPAEAAAAADVVITMLPDDAAVEEVLLGED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  81 GAFAGMERGAIFVDHTTVSAQVTRELAAEADGLGLGFVDAPVSGGQAGAENGVLSIMCGGSEAHYAAAEPVMAAYARVCR 160
Cdd:COG2084   80 GLLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405 161 RLGESGSGQIAKMMNQICIAGLVQGLAEALAFGEKAGMDGKAVVEVISQGAAGSWQMANRHGSMLDGKFDYGFAVDWMRK 240
Cdd:COG2084  160 HVGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLK 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 500166405 241 DLGICLRTADEVGASLPVTALVDQFYKEVQQMGGGRWDTSALIKRL 286
Cdd:COG2084  240 DLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-286 2.83e-116

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 335.55  E-value: 2.83e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   1 MAKLAFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAAQhGGRAAATPAEAAEGAAFVMACVGNDDDLRSICRGES 80
Cdd:COG2084    1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAA-GARVAASPAEAAAAADVVITMLPDDAAVEEVLLGED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  81 GAFAGMERGAIFVDHTTVSAQVTRELAAEADGLGLGFVDAPVSGGQAGAENGVLSIMCGGSEAHYAAAEPVMAAYARVCR 160
Cdd:COG2084   80 GLLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405 161 RLGESGSGQIAKMMNQICIAGLVQGLAEALAFGEKAGMDGKAVVEVISQGAAGSWQMANRHGSMLDGKFDYGFAVDWMRK 240
Cdd:COG2084  160 HVGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLK 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 500166405 241 DLGICLRTADEVGASLPVTALVDQFYKEVQQMGGGRWDTSALIKRL 286
Cdd:COG2084  240 DLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-284 6.84e-56

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 182.17  E-value: 6.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   1 MAKLAFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAAqHGGRAAATPAEAAEGAAFVMACVGNDDDLRSICRGES 80
Cdd:PRK11559   2 TMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIA-AGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  81 GAFAGMERGAIFVDHTTVSAQVTRELAAEADGLGLGFVDAPVSGGQAGAENGVLSIMCGGSEAHYAAAEPVMAAYARVCR 160
Cdd:PRK11559  81 GIIEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405 161 RLGESGSGQIAKMMNQICIAGLVQGLAEALAFGEKAGMDGKAVVEVISQGAAGSWQMANRHGSMLDGKFDYGFAVDWMRK 240
Cdd:PRK11559 161 HTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 500166405 241 DLGICLRTADEVGASLPVTALVDQFYKEVQQMGGGRWDTSALIK 284
Cdd:PRK11559 241 DLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALAC 284
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 3-163 5.23e-51

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: 164.95  E-value: 5.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405    3 KLAFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAAQhGGRAAATPAEAAEGAAFVMACVGNDDDLRSICRGEsGA 82
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAA-GAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   83 FAGMERGAIFVDHTTVSAQVTRELAAEADGLGLGFVDAPVSGGQAGAENGVLSIMCGGSEAHYAAAEPVMAAYARVCRRL 162
Cdd:pfam03446  79 LPGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYI 158


                  .
gi 500166405  163 G 163
Cdd:pfam03446 159 G 159
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 6-286 2.50e-46

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: 157.27  E-value: 2.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405    6 FLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAAQhGGRAAATPAEAAEGAAFVMACVGNDDDLRSICRGESGAFAG 85
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAA-GAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   86 MERGAIFVDHTTVSAQVTRELAAEADGLGLGFVDAPVSGGQAGAENGVLSIMCGGSEAHYAAAEPVMAAYARVCRRLGES 165
Cdd:TIGR01692  80 VAKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  166 GSGQIAKMMNQICIAGLVQGLAEALAFGEKAGMDGKAVVEVISQGAAGSWQMANRH-------GSMLDGKFDYGFAVDWM 238
Cdd:TIGR01692 160 GAGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNpvpgvmpQAPASNGYQGGFGTALM 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 500166405  239 RKDLGICLRTADEVGASLPVTALVDQFYKEVQQMGGGRWDTSALIKRL 286
Cdd:TIGR01692 240 LKDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
 4-42 8.03e-03

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


Pssm-ID: 187576 [Multi-domain]  Cd Length: 251  Bit Score: 36.91  E-value: 8.03e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 500166405   4 LAFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAA 42
Cdd:cd05266    1 VLILGCGYLGQRLARQLLAQGWQVTGTTRSPEKLAADRP 39
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-286 2.83e-116

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 335.55  E-value: 2.83e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   1 MAKLAFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAAQhGGRAAATPAEAAEGAAFVMACVGNDDDLRSICRGES 80
Cdd:COG2084    1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAA-GARVAASPAEAAAAADVVITMLPDDAAVEEVLLGED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  81 GAFAGMERGAIFVDHTTVSAQVTRELAAEADGLGLGFVDAPVSGGQAGAENGVLSIMCGGSEAHYAAAEPVMAAYARVCR 160
Cdd:COG2084   80 GLLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405 161 RLGESGSGQIAKMMNQICIAGLVQGLAEALAFGEKAGMDGKAVVEVISQGAAGSWQMANRHGSMLDGKFDYGFAVDWMRK 240
Cdd:COG2084  160 HVGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLK 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 500166405 241 DLGICLRTADEVGASLPVTALVDQFYKEVQQMGGGRWDTSALIKRL 286
Cdd:COG2084  240 DLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-284 6.84e-56

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 182.17  E-value: 6.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   1 MAKLAFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAAqHGGRAAATPAEAAEGAAFVMACVGNDDDLRSICRGES 80
Cdd:PRK11559   2 TMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIA-AGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  81 GAFAGMERGAIFVDHTTVSAQVTRELAAEADGLGLGFVDAPVSGGQAGAENGVLSIMCGGSEAHYAAAEPVMAAYARVCR 160
Cdd:PRK11559  81 GIIEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405 161 RLGESGSGQIAKMMNQICIAGLVQGLAEALAFGEKAGMDGKAVVEVISQGAAGSWQMANRHGSMLDGKFDYGFAVDWMRK 240
Cdd:PRK11559 161 HTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 500166405 241 DLGICLRTADEVGASLPVTALVDQFYKEVQQMGGGRWDTSALIK 284
Cdd:PRK11559 241 DLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALAC 284
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 3-163 5.23e-51

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: 164.95  E-value: 5.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405    3 KLAFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAAQhGGRAAATPAEAAEGAAFVMACVGNDDDLRSICRGEsGA 82
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAA-GAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   83 FAGMERGAIFVDHTTVSAQVTRELAAEADGLGLGFVDAPVSGGQAGAENGVLSIMCGGSEAHYAAAEPVMAAYARVCRRL 162
Cdd:pfam03446  79 LPGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYI 158


                  .
gi 500166405  163 G 163
Cdd:pfam03446 159 G 159
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 6-286 2.50e-46

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: 157.27  E-value: 2.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405    6 FLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAAQhGGRAAATPAEAAEGAAFVMACVGNDDDLRSICRGESGAFAG 85
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAA-GAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   86 MERGAIFVDHTTVSAQVTRELAAEADGLGLGFVDAPVSGGQAGAENGVLSIMCGGSEAHYAAAEPVMAAYARVCRRLGES 165
Cdd:TIGR01692  80 VAKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  166 GSGQIAKMMNQICIAGLVQGLAEALAFGEKAGMDGKAVVEVISQGAAGSWQMANRH-------GSMLDGKFDYGFAVDWM 238
Cdd:TIGR01692 160 GAGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNpvpgvmpQAPASNGYQGGFGTALM 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 500166405  239 RKDLGICLRTADEVGASLPVTALVDQFYKEVQQMGGGRWDTSALIKRL 286
Cdd:TIGR01692 240 LKDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
3-286 1.16e-43

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 150.56  E-value: 1.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   3 KLAFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAaqHGGRAAATPAEAAEGAAFVMACVGNDDDLRSICRGESGA 82
Cdd:PRK15059   2 KLGFIGLGIMGTPMAINLARAGHQLHVTTIGPVADELLS--LGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  83 FAGMERGAIFVDHTTVSAQVTRELAAEADGLGLGFVDAPVSGGQAGAENGVLSIMCGGSEAHYAAAEPVMAAYARVCRRL 162
Cdd:PRK15059  80 TKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405 163 GESGSGQIAKMMNQICIAGLVQGLAEALAFGEKAGMDGKAVVEVISQGAAGSwQMANRHGS-MLDGKFDYGFAVDWMRKD 241
Cdd:PRK15059 160 GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASS-RILEVHGErMIKRTFNPGFKIALHQKD 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 500166405 242 LGICLRTADEVGASLPVTALVDQFYKEVQQMGGGRWDTSALIKRL 286
Cdd:PRK15059 239 LNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQAL 283
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
1-286 7.81e-41

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 143.07  E-value: 7.81e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   1 MAKLAFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAAQhGGRAAATPAEAAEGAAFVMACVGNDDDLRSICRGES 80
Cdd:PRK15461   1 MAAIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDK-GATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGEN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  81 GAFAGMERGAIFVDHTTVSAQVTRELAAEADGLGLGFVDAPVSGGQAGAENGVLSIMCGGSEAHYAAAEPVMAAYARVCR 160
Cdd:PRK15461  80 GVCEGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405 161 RLGESGSGQIAKMMNQICIAGLVQGLAEALAFGEKAGMDGKAVVEVISQGAAGSWQMANRH-GSMLDGKFDYGFAVDWMR 239
Cdd:PRK15461 160 NAGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALGLSFDVALKVMSGTAAGKGHFTTTWpNKVLKGDLSPAFMIDLAH 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 500166405 240 KDLGICLRTADEVGASLPVTALVDQFYKEVQQMGGGRWDTSALIKRL 286
Cdd:PRK15461 240 KDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQV 286
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 166-286 1.35e-37

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: 129.18  E-value: 1.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  166 GSGQIAKMMNQICIAGLVQGLAEALAFGEKAGMDGKAVVEVISQGAAGSWQMANRHG-SMLDGKFDYGFAVDWMRKDLGI 244
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFPqRVLSRDFDPGFALDLMLKDLGL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 500166405  245 CLRTADEVGASLPVTALVDQFYKEVQQMGGGRWDTSALIKRL 286
Cdd:pfam14833  81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
PLN02858 PLN02858
fructose-bisphosphate aldolase
 3-284 2.18e-37

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 140.76  E-value: 2.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405    3 KLAFLGLGVMGFPMAGHLAARGHEVTVYNRS-PAKAEAwaAQHGGRAAATPAEAAEGAAFVMACVGNDDDLRSICRGESG 81
Cdd:PLN02858  326 RIGFIGLGAMGFGMASHLLKSNFSVCGYDVYkPTLVRF--ENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLG 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   82 AFAGMERGAIFVDHTTVS----AQVTRELAAEADGLGLgfVDAPVSGGQAGAENGVLSIMCGGSEAHYAAAEPVMAAYAR 157
Cdd:PLN02858  404 AVSALPAGASIVLSSTVSpgfvIQLERRLENEGRDIKL--VDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSE 481

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  158 VCRRL-GESGSGQIAKMMNQIcIAGL-VQGLAEALAFGEKAGMDGKAVVEVISQGAAGSWQMANRHGSMLDGKFDYGFAV 235
Cdd:PLN02858  482 KLYVIkGGCGAGSGVKMVNQL-LAGVhIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSAL 560

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 500166405  236 DWMRKDLGICLRTADEVGASLPVTALVDQFYKEVQQMGGGRWDTSALIK 284
Cdd:PLN02858  561 DIFVKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVK 609
PLN02858 PLN02858
fructose-bisphosphate aldolase
 2-264 4.94e-25

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 104.93  E-value: 4.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405    2 AKLAFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAAQHGGRAAATPAEAAEGAAFVMAcVGNDDDLRSICRGESG 81
Cdd:PLN02858    5 GVVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVV-LSHPDQVDDVFFGDEG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   82 AFAGMERGAIFVDHTTVSAQVTRELAAE--ADGLGLGFVDAPVSGGQAGAENGVLSIMCGGSEAHYAAAEPVMAAyarVC 159
Cdd:PLN02858   84 AAKGLQKGAVILIRSTILPLQLQKLEKKltERKEQIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSA---MC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  160 RRL----GESGSGQIAKMMNQICIAGLVQGLAEALAFGEKAGMDGKAVVEVISQGAAGSWQMANRHGSMLDGKFDYGFAV 235
Cdd:PLN02858  161 QKLytfeGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRFL 240

                         250       260
                  ....*....|....*....|....*....
gi 500166405  236 DWMRKDLGICLRTADEVGASLPVTALVDQ 264
Cdd:PLN02858  241 NVLVQNLGIVLDMAKSLPFPLPLLAVAHQ 269
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
3-217 1.78e-14

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 72.09  E-value: 1.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   3 KLAFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAwAAQHGgraaatpaeaaegaafvMACVGNDDDLRSICRGESGA 82
Cdd:PRK09599   2 QLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEA-LAEEG-----------------ATGADSLEELVAKLPAPRVV 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  83 F----AG-------------MERGAIFVD----HTTVSAQVTRELAAEadglGLGFVDAPVSGGQAGAENGVlSIMCGGS 141
Cdd:PRK09599  64 WlmvpAGeitdatidelaplLSPGDIVIDggnsYYKDDIRRAELLAEK----GIHFVDVGTSGGVWGLERGY-CLMIGGD 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405 142 EAHYAAAEPVMAAYArVCR-----RLGESGSGQIAKMM-NQICIaGLVQGLAEALAFGEKAG--MDGKAVVEVISQGAA- 212
Cdd:PRK09599 139 KEAVERLEPIFKALA-PRAedgylHAGPVGAGHFVKMVhNGIEY-GMMQAYAEGFELLEASRfdLDLAAVAEVWRRGSVi 216


                 ....*
gi 500166405 213 GSWQM 217
Cdd:PRK09599 217 RSWLL 221
YqeC COG1023
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
3-223 2.02e-14

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


Pssm-ID: 440646 [Multi-domain]  Cd Length: 300  Bit Score: 71.66  E-value: 2.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   3 KLAFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAwAAQHGGRAaatpaeaaegaafvmacVGNDDDLRS-------- 74
Cdd:COG1023    2 QIGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAA-LAAEGATG-----------------ADSLEELVAklpaprvv 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  75 --------ICRGESGAFAG-MERGAIFVD------HTTVsaqvtrELAAEADGLGLGFVDAPVSGGQAGAENGvLSIMCG 139
Cdd:COG1023   64 wlmvpageITDQVIEELAPlLEPGDIVIDggnsnyKDDI------RRAEELAEKGIHFVDVGTSGGVWGLENG-YCLMIG 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405 140 GSEAHYAAAEPVMAAYA----RVCRRLGESGSGQIAKMM-NQIcIAGLVQGLAEALAFGEKA--GMDGKAVVEVisqgaa 212
Cdd:COG1023  137 GDKEAVERLEPIFKALApgaeNGYLHCGPVGAGHFVKMVhNGI-EYGMMQAYAEGFELLEASefDLDLAEVAEV------ 209

                        250
                 ....*....|.
gi 500166405 213 gsWqmanRHGS 223
Cdd:COG1023  210 --W----RRGS 214
PLN02350 PLN02350
phosphogluconate dehydrogenase (decarboxylating)
 8-189 3.09e-09

phosphogluconate dehydrogenase (decarboxylating)


Pssm-ID: 215200 [Multi-domain]  Cd Length: 493  Bit Score: 57.42  E-value: 3.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   8 GLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAW---AAQHGGRAAATPAEAAEGAA----------FVMACVGNDDDLRS 74
Cdd:PLN02350  13 GLAVMGQNLALNIAEKGFPISVYNRTTSKVDETverAKKEGNLPLYGFKDPEDFVLsiqkprsviiLVKAGAPVDQTIKA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  75 ICrgesgafAGMERGAIFVDHTTVSAQVTRELAAEADGLGLGFVDAPVSGGQAGAENGVlSIMCGGSEAHYAAAEP-VMA 153
Cdd:PLN02350  93 LS-------EYMEPGDCIIDGGNEWYENTERRIKEAAEKGLLYLGMGVSGGEEGARNGP-SLMPGGSFEAYKNIEDiLEK 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 500166405 154 AYARV----C-RRLGESGSGQIAKMMNQICIAGLVQGLAEA 189
Cdd:PLN02350 165 VAAQVddgpCvTYIGPGGAGNFVKMVHNGIEYGDMQLISEA 205
Gnd COG0362
6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate ...
 1-173 3.36e-09

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: 57.01  E-value: 3.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   1 MAKLAFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAAQHGgraaatpaeaaEGAAFVMAcvgndDDLRsicrges 80
Cdd:COG0362    2 KADIGVIGLAVMGRNLALNIADHGFSVAVYNRTAEKTDAFLAEHG-----------KGKNIVGT-----YSLE------- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  81 gAF---------------AG-------------MERGAIFVD----HTTVSAQVTRELAAEadglGLGFVDAPVSGGQAG 128
Cdd:COG0362   59 -EFvaslerprkillmvkAGkpvdavieqllplLEPGDIIIDggnsHFTDTIRREKELAEK----GIHFIGMGVSGGEEG 133

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 500166405 129 AENGVlSIMCGGSEAHYAAAEPVM-AAYARV-----CRRLGESGSGQIAKM 173
Cdd:COG0362  134 ALHGP-SIMPGGSKEAYELVKPILeAIAAKVdgepcVTYIGPDGAGHFVKM 183
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 1-277 6.95e-08

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 53.25  E-value: 6.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   1 MAKLAFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAAQHGgraaatpaeaaeGAAFVMACVGNDDDL-RSICR-- 77
Cdd:PTZ00142   1 MSDIGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEEFVKKAK------------EGNTRVKGYHTLEELvNSLKKpr 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  78 --------GE------SGAFAGMERGAIFVDHTTVSAQVTRELAAEADGLGLGFVDAPVSGGQAGAENGVlSIMCGGSEA 143
Cdd:PTZ00142  69 kvillikaGEavdetiDNLLPLLEKGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGP-SLMPGGNKE 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405 144 HYAAAEPVM-AAYARV-----CRRLGESGSGQIAKMMNQICIAGLVQGLAEALAFGEKA-GMDGKAVVEVISqgaagSWq 216
Cdd:PTZ00142 148 AYDHVKDILeKCSAKVgdspcVTYVGPGSSGHYVKMVHNGIEYGDMQLISESYKLMKHIlGMSNEELSEVFN-----KW- 221

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500166405 217 manrHGSMLDgkfdyGFAVDWMRKDLGICLRTADEvgaslpvtALVDQFYKEVQQMGGGRW 277
Cdd:PTZ00142 222 ----NEGILN-----SYLIEITAKILAKKDDLGEE--------HLVDKILDIAGSKGTGKW 265
PRK09287 PRK09287
NADP-dependent phosphogluconate dehydrogenase;
12-173 6.09e-07

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236453 [Multi-domain]  Cd Length: 459  Bit Score: 50.12  E-value: 6.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  12 MGFPMAGHLAARGHEVTVYNRSPAKAEAWAAQHGgrAAATPAEAAEGAAF-------------VMACVGNDDDLRSIcrg 78
Cdd:PRK09287   1 MGKNLALNIASHGYTVAVYNRTPEKTDEFLAEEG--KGKKIVPAYTLEEFvaslekprkillmVKAGAPVDAVIEQL--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405  79 esgaFAGMERGAIFVD----HTTVSAQVTRELAAEadglGLGFVDAPVSGGQAGAENGVlSIMCGGSEAHYAAAEPVM-A 153
Cdd:PRK09287  76 ----LPLLEKGDIIIDggnsNYKDTIRREKELAEK----GIHFIGMGVSGGEEGALHGP-SIMPGGQKEAYELVAPILeK 146

                        170       180
                 ....*....|....*....|....*.
gi 500166405 154 AYARV------CRRLGESGSGQIAKM 173
Cdd:PRK09287 147 IAAKVedgepcVTYIGPDGAGHYVKM 172
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-45 3.40e-05

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: 44.28  E-value: 3.40e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 500166405   1 MAKLAFLGLGVMGFPMAGHLAARG---HEVTVYNRSPAKAEAWAAQHG 45
Cdd:COG0345    2 SMKIGFIGAGNMGSAIIKGLLKSGvppEDIIVSDRSPERLEALAERYG 49
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
5-47 4.25e-05

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


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 43.62  E-value: 4.25e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 500166405   5 AFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAAQHGGR 47
Cdd:COG2085    2 GIIGTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAELGPG 44
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-45 2.59e-04

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 41.67  E-value: 2.59e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 500166405   1 MAKLAFLGLGVMGFPMAGHLAARG---HEVTVYNRSPAKAEAWAAQHG 45
Cdd:PRK11880   2 MKKIGFIGGGNMASAIIGGLLASGvpaKDIIVSDPSPEKRAALAEEYG 49
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 1-46 4.80e-04

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 39.48  E-value: 4.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 500166405    1 MAKLAFLGLGVMGFPMAGHLAARG-HEVTVYNRSPAKAEAWAAQHGG 46
Cdd:pfam01488  12 DKKVLLIGAGEMGELVAKHLLAKGaKEVTIANRTIERAQELAEKFGG 58
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 3-47 2.11e-03

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 39.40  E-value: 2.11e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 500166405   3 KLAFLGLGVMGFPMAGHLAARG-HEVTVYNRSPAKAEAWAAQHGGR 47
Cdd:PRK00045 184 KVLVIGAGEMGELVAKHLAEKGvRKITVANRTLERAEELAEEFGGE 229
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-96 2.28e-03

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 39.02  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500166405   1 MAKLAFLGLGVMGFPMAGHLAARGHEVT-VYNRSPAKAEAWAAQHGGRAAATPAEAAEGAAFVMACVgNDDDLRSICRG- 78
Cdd:COG5495    3 RMKIGIIGAGRVGTALAAALRAAGHEVVgVYSRSPASAERAAALLGAVPALDLEELAAEADLVLLAV-PDDAIAEVAAGl 81

                         90
                 ....*....|....*....
gi 500166405  79 -ESGAFAgmeRGAIFVdHT 96
Cdd:COG5495   82 aAAGALR---PGQLVV-HT 96
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 3-28 2.33e-03

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 39.13  E-value: 2.33e-03
                          10        20
                  ....*....|....*....|....*.
gi 500166405    3 KLAFLGLGVMGFPMAGHLAARGHEVT 28
Cdd:TIGR03026   2 KIAVIGLGYVGLPLAALLADLGHDVT 27
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
5-47 4.63e-03

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 35.67  E-value: 4.63e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 500166405    5 AFLGLGVMGFPMAGHLAARG-HEVTV-YNRSPAKAEAWAAQHGGR 47
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGpHEVVVaNSRNPEKAEELAEEYGVG 45
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 3-47 4.73e-03

Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440142 [Multi-domain]  Cd Length: 425  Bit Score: 38.17  E-value: 4.73e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 500166405   3 KLAFLGLGVMGFPMAGHLAARG-HEVTVYNRSPAKAEAWAAQHGGR 47
Cdd:COG0373  184 TVLVIGAGEMGELAARHLAAKGvKRITVANRTLERAEELAEEFGGE 229
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
 4-42 8.03e-03

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


Pssm-ID: 187576 [Multi-domain]  Cd Length: 251  Bit Score: 36.91  E-value: 8.03e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 500166405   4 LAFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAA 42
Cdd:cd05266    1 VLILGCGYLGQRLARQLLAQGWQVTGTTRSPEKLAADRP 39
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
1-44 8.64e-03

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 36.97  E-value: 8.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 500166405   1 MAKLAFLGLGVMGFPMAGHLAARGHEVTVYNRSPAKAEAWAAQH 44
Cdd:PRK00094   1 MMKIAVLGAGSWGTALAIVLARNGHDVTLWARDPEQAAEINADR 44
 
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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