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Conserved domains on  [gi|1815996340|ref|WP_163142956|]
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MULTISPECIES: NAD(P)-dependent oxidoreductase [Bacillaceae]

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 ...
 9-290 3.73e-130

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


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 370.99  E-value: 3.73e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   9 IGFVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWAETPAAVAKKANVIITIVGYPADVEEVYLGENGIIT 88
Cdd:COG2084     4 VGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  89 NGRENTYVIDMTTSTPTLAKRIYEEARKIGIYAIDAPVSGGDIGARDAKLSIMAGGDRDAFLAVEPIFNLLGTNIVYQGN 168
Cdd:COG2084    84 ALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVGD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340 169 AGAGQHTKMCNQIAIASNMIGVCEAVVYAEKAGLDPKTVLQSITSGAAGSWSLSNLAPRMIEGNFEPGFYIKHFIKDMNI 248
Cdd:COG2084   164 AGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDLGL 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1815996340 249 ALNEAEAMGMMTPGLSLAKKMYAELAENGEENSGTQALYKYW 290
Cdd:COG2084   244 ALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 9-290 3.73e-130

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 370.99  E-value: 3.73e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   9 IGFVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWAETPAAVAKKANVIITIVGYPADVEEVYLGENGIIT 88
Cdd:COG2084     4 VGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  89 NGRENTYVIDMTTSTPTLAKRIYEEARKIGIYAIDAPVSGGDIGARDAKLSIMAGGDRDAFLAVEPIFNLLGTNIVYQGN 168
Cdd:COG2084    84 ALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVGD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340 169 AGAGQHTKMCNQIAIASNMIGVCEAVVYAEKAGLDPKTVLQSITSGAAGSWSLSNLAPRMIEGNFEPGFYIKHFIKDMNI 248
Cdd:COG2084   164 AGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDLGL 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1815996340 249 ALNEAEAMGMMTPGLSLAKKMYAELAENGEENSGTQALYKYW 290
Cdd:COG2084   244 ALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 9-292 3.36e-88

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 264.99  E-value: 3.36e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   9 IGFVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWAETPAAVAKKANVIITIVGYPADVEEVYLGENGIIT 88
Cdd:PRK11559    5 VGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGIIE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  89 NGRENTYVIDMTTSTPTLAKRIYEEARKIGIYAIDAPVSGGDIGARDAKLSIMAGGDRDAFLAVEPIFNLLGTNIVYQGN 168
Cdd:PRK11559   85 GAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTGD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340 169 AGAGQHTKMCNQIAIASNMIGVCEAVVYAEKAGLDPKTVLQSITSGAAGSWSLSNLAPRMIEGNFEPGFYIKHFIKDMNI 248
Cdd:PRK11559  165 IGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDLAN 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1815996340 249 ALNEAEAMGMMTPGLSLAKKMYAELAENGEENSGTQALYKYWEK 292
Cdd:PRK11559  245 ALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEK 288
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 9-167 2.70e-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: 199.23  E-value: 2.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   9 IGFVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWAETPAAVAKKANVIITIVGYPADVEEVYLGEnGIIT 88
Cdd:pfam03446   2 IGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLLP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1815996340  89 NGRENTYVIDMTTSTPTLAKRIYEEARKIGIYAIDAPVSGGDIGARDAKLSIMAGGDRDAFLAVEPIFNLLGTNIVYQG 167
Cdd:pfam03446  81 GLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 11-288 4.67e-63

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: 200.41  E-value: 4.67e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  11 FVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWAETPAAVAKKANVIITIVGYPADVEEVYLGENGIITNG 90
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  91 RENTYVIDMTTSTPTLAKRIYEEARKIGIYAIDAPVSGGDIGARDAKLSIMAGGDRDAFLAVEPIFNLLGTNIVYQGNAG 170
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340 171 AGQHTKMCNQIAIASNMIGVCEAVVYAEKAGLDPKTVLQSITSGAAGSWSLS--NLAPRMIEG-----NFEPGFYIKHFI 243
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDtyNPVPGVMPQapasnGYQGGFGTALML 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1815996340 244 KDMNIALNEAEAMGMMTPGLSLAKKMYAELAENG---EENSGTQALYK 288
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGhggKDFSSVIQLLR 288
NmrA_TMR_like_1_SDR_a cd05231
NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, ...
 8-51 6.12e-04

NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, subgroup 1, atypical (a) SDRs; Atypical SDRs related to NMRa, TMR, and HSCARG (an NADPH sensor). This subgroup resembles the SDRs and has a partially conserved characteristic [ST]GXXGXXG NAD-binding motif, but lacks the conserved active site residues. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. 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. Atypical SDRs are distinct from classical SDRs. 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: 187542 [Multi-domain]  Cd Length: 259  Bit Score: 40.39  E-value: 6.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1815996340   8 VIGfvGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAE 51
Cdd:cd05231     3 VTG--ATGRIGSKVATTLLEAGRPVRALVRSDERAAALAARGAE 44
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 9-290 3.73e-130

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 370.99  E-value: 3.73e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   9 IGFVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWAETPAAVAKKANVIITIVGYPADVEEVYLGENGIIT 88
Cdd:COG2084     4 VGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  89 NGRENTYVIDMTTSTPTLAKRIYEEARKIGIYAIDAPVSGGDIGARDAKLSIMAGGDRDAFLAVEPIFNLLGTNIVYQGN 168
Cdd:COG2084    84 ALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVGD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340 169 AGAGQHTKMCNQIAIASNMIGVCEAVVYAEKAGLDPKTVLQSITSGAAGSWSLSNLAPRMIEGNFEPGFYIKHFIKDMNI 248
Cdd:COG2084   164 AGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDLGL 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1815996340 249 ALNEAEAMGMMTPGLSLAKKMYAELAENGEENSGTQALYKYW 290
Cdd:COG2084   244 ALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 9-292 3.36e-88

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 264.99  E-value: 3.36e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   9 IGFVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWAETPAAVAKKANVIITIVGYPADVEEVYLGENGIIT 88
Cdd:PRK11559    5 VGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGIIE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  89 NGRENTYVIDMTTSTPTLAKRIYEEARKIGIYAIDAPVSGGDIGARDAKLSIMAGGDRDAFLAVEPIFNLLGTNIVYQGN 168
Cdd:PRK11559   85 GAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTGD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340 169 AGAGQHTKMCNQIAIASNMIGVCEAVVYAEKAGLDPKTVLQSITSGAAGSWSLSNLAPRMIEGNFEPGFYIKHFIKDMNI 248
Cdd:PRK11559  165 IGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDLAN 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1815996340 249 ALNEAEAMGMMTPGLSLAKKMYAELAENGEENSGTQALYKYWEK 292
Cdd:PRK11559  245 ALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEK 288
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 9-167 2.70e-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: 199.23  E-value: 2.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   9 IGFVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWAETPAAVAKKANVIITIVGYPADVEEVYLGEnGIIT 88
Cdd:pfam03446   2 IGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLLP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1815996340  89 NGRENTYVIDMTTSTPTLAKRIYEEARKIGIYAIDAPVSGGDIGARDAKLSIMAGGDRDAFLAVEPIFNLLGTNIVYQG 167
Cdd:pfam03446  81 GLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
9-286 9.90e-64

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 202.17  E-value: 9.90e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   9 IGFVGTGVMGKSMAGHLLKAGYPLVVyTRTKEKASELIEKGAEWAETPAAVAKKANVIITIVGYPADVEEVYLGENGIIT 88
Cdd:PRK15059    3 LGFIGLGIMGTPMAINLARAGHQLHV-TTIGPVADELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGCTK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  89 NGRENTYVIDMTTSTPTLAKRIYEEARKIGIYAIDAPVSGGDIGARDAKLSIMAGGDRDAFLAVEPIFNLLGTNIVYQGN 168
Cdd:PRK15059   82 ASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340 169 AGAGQHTKMCNQIAIASNMIGVCEAVVYAEKAGLDPKTVLQSITSGAAGSWSLSNLAPRMIEGNFEPGFYIKHFIKDMNI 248
Cdd:PRK15059  162 NGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDLNL 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1815996340 249 ALNEAEAMGMMTPGLSLAKKMYAELAENG----EENSGTQAL 286
Cdd:PRK15059  242 ALQSAKALALNLPNTATCQELFNTCAANGgsqlDHSALVQAL 283
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 11-288 4.67e-63

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: 200.41  E-value: 4.67e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  11 FVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWAETPAAVAKKANVIITIVGYPADVEEVYLGENGIITNG 90
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  91 RENTYVIDMTTSTPTLAKRIYEEARKIGIYAIDAPVSGGDIGARDAKLSIMAGGDRDAFLAVEPIFNLLGTNIVYQGNAG 170
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340 171 AGQHTKMCNQIAIASNMIGVCEAVVYAEKAGLDPKTVLQSITSGAAGSWSLS--NLAPRMIEG-----NFEPGFYIKHFI 243
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDtyNPVPGVMPQapasnGYQGGFGTALML 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1815996340 244 KDMNIALNEAEAMGMMTPGLSLAKKMYAELAENG---EENSGTQALYK 288
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGhggKDFSSVIQLLR 288
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 170-290 1.60e-43

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: 144.59  E-value: 1.60e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340 170 GAGQHTKMCNQIAIASNMIGVCEAVVYAEKAGLDPKTVLQSITSGAAGSWSLSNLAP-RMIEGNFEPGFYIKHFIKDMNI 248
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFPqRVLSRDFDPGFALDLMLKDLGL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1815996340 249 ALNEAEAMGMMTPGLSLAKKMYAELAENGEENSGTQALYKYW 290
Cdd:pfam14833  81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
PLN02858 PLN02858
fructose-bisphosphate aldolase
 9-270 1.29e-37

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 141.53  E-value: 1.29e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340    9 IGFVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWAETPAAVAKKANVIITIVGYPADVEEVYLGENGIIT 88
Cdd:PLN02858   327 IGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAVS 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   89 NGRENTYVIDMTTSTP----TLAKRIYEEARkiGIYAIDAPVSGGDIGARDAKLSIMAGGDRDAFLAVEPIFNLLGTNI- 163
Cdd:PLN02858   407 ALPAGASIVLSSTVSPgfviQLERRLENEGR--DIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKLy 484

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  164 VYQGNAGAGQHTKMCNQIAIASNMIGVCEAVVYAEKAGLDPKTVLQSITSGAAGSWSLSNLAPRMIEGNFEPGFYIKHFI 243
Cdd:PLN02858   485 VIKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALDIFV 564

                          250       260
                   ....*....|....*....|....*..
gi 1815996340  244 KDMNIALNEAEAMGMMTPGLSLAKKMY 270
Cdd:PLN02858   565 KDLGIVSREGSSRKIPLHLSTVAHQLF 591
PLN02858 PLN02858
fructose-bisphosphate aldolase
 8-292 8.40e-36

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 136.13  E-value: 8.40e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340    8 VIGFVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWAETPAAVAKKANVIITIVGYPADVEEVYLGENGII 87
Cdd:PLN02858     6 VVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFGDEGAA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   88 TNGRENTYVIDMTTSTPT----LAKRIYEEarKIGIYAIDAPVSGGDIGARDAKLSIMAGGDRDAFLAVEPIFNLLGTNI 163
Cdd:PLN02858    86 KGLQKGAVILIRSTILPLqlqkLEKKLTER--KEQIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  164 -VYQGNAGAGQHTKMCNQIAIASNMIGVCEAVVYAEKAGLDPKTVLQSITSGAAGSWSLSNLAPRMIEGNFEPGFYIKHF 242
Cdd:PLN02858   164 yTFEGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRFLNVL 243

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1815996340  243 IKDMNIALNEAEAMGMMTPGLSLAKKMYAELAENGEENSGTQALYKYWEK 292
Cdd:PLN02858   244 VQNLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKVWEK 293
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
8-287 2.13e-33

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 123.81  E-value: 2.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   8 VIGFVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWAETPAAVAKKANVIITIVGYPADVEEVYLGENGII 87
Cdd:PRK15461    3 AIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  88 TNGRENTYVIDMTTSTPTLAKRIYEEARKIGIYAIDAPVSGGDIGARDAKLSIMAGGDRDAFLAVEPIFNLLGTNIVYQG 167
Cdd:PRK15461   83 EGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340 168 NAGAGQHTKMCNQ-IAIASNMIGVcEAVVYAEKAGLDPKTVLQSITSGAAGSWSLSNLAP-RMIEGNFEPGFYIKHFIKD 245
Cdd:PRK15461  163 GPGMGIRVKLINNyMSIALNALSA-EAAVLCEALGLSFDVALKVMSGTAAGKGHFTTTWPnKVLKGDLSPAFMIDLAHKD 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1815996340 246 MNIALNEAEAMGMMTPGLSLAKKMYAELAENGEENSGTQALY 287
Cdd:PRK15461  242 LGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAIL 283
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
9-177 4.82e-18

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 82.10  E-value: 4.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   9 IGFVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWAETPAAVAKKAN---VIITIV--GYPAD--VEEV-- 79
Cdd:PRK09599    3 LGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPaprVVWLMVpaGEITDatIDELap 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  80 YLGENGIITNGrENTYVIDmttstptlAKRIYEEARKIGIYAIDAPVSGGDIGARDAkLSIMAGGDRDAFLAVEPIFNLL 159
Cdd:PRK09599   83 LLSPGDIVIDG-GNSYYKD--------DIRRAELLAEKGIHFVDVGTSGGVWGLERG-YCLMIGGDKEAVERLEPIFKAL 152

                         170       180
                  ....*....|....*....|..
gi 1815996340 160 GTNI----VYQGNAGAGQHTKM 177
Cdd:PRK09599  153 APRAedgyLHAGPVGAGHFVKM 174
YqeC COG1023
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
9-177 1.48e-17

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


Pssm-ID: 440646 [Multi-domain]  Cd Length: 300  Bit Score: 80.91  E-value: 1.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   9 IGFVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWAETPAAVAKKAN---VIITIVgyPAD--VEEV---- 79
Cdd:COG1023     3 IGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKLPaprVVWLMV--PAGeiTDQVieel 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  80 --YLGENGIITNGrENTYVIDmttstptlAKRIYEEARKIGIYAIDAPVSGGDIGARDAkLSIMAGGDRDAFLAVEPIFN 157
Cdd:COG1023    81 apLLEPGDIVIDG-GNSNYKD--------DIRRAEELAEKGIHFVDVGTSGGVWGLENG-YCLMIGGDKEAVERLEPIFK 150

                         170       180
                  ....*....|....*....|....
gi 1815996340 158 LLGTNI----VYQGNAGAGQHTKM 177
Cdd:COG1023   151 ALAPGAengyLHCGPVGAGHFVKM 174
Gnd COG0362
6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate ...
 9-177 2.07e-13

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: 69.72  E-value: 2.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   9 IGFVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEW-----AETPAA-VA--KKANVIITIV--GYPAD--V 76
Cdd:COG0362     5 IGVIGLAVMGRNLALNIADHGFSVAVYNRTAEKTDAFLAEHGKGknivgTYSLEEfVAslERPRKILLMVkaGKPVDavI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  77 EEV--YLGENGIITNGrENTYVIDmttstpTlaKRIYEEARKIGIYAIDAPVSGGDIGARDAKlSIMAGGDRDAFLAVEP 154
Cdd:COG0362    85 EQLlpLLEPGDIIIDG-GNSHFTD------T--IRREKELAEKGIHFIGMGVSGGEEGALHGP-SIMPGGSKEAYELVKP 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1815996340 155 IFnllgTNI----------VYQGNAGAGQHTKM 177
Cdd:COG0362   155 IL----EAIaakvdgepcvTYIGPDGAGHFVKM 183
PLN02350 PLN02350
phosphogluconate dehydrogenase (decarboxylating)
 1-177 5.86e-13

phosphogluconate dehydrogenase (decarboxylating)


Pssm-ID: 215200 [Multi-domain]  Cd Length: 493  Bit Score: 68.59  E-value: 5.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   1 MVSPENTVIGFVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWAETP-----------AAVAKKANVIITI 69
Cdd:PLN02350    1 MASAALSRIGLAGLAVMGQNLALNIAEKGFPISVYNRTTSKVDETVERAKKEGNLPlygfkdpedfvLSIQKPRSVIILV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  70 -VGYPADVE----EVYLGENGIITNG----RENTyvidmttstptlAKRIyEEARKIGIYAIDAPVSGGDIGARDAKlSI 140
Cdd:PLN02350   81 kAGAPVDQTikalSEYMEPGDCIIDGgnewYENT------------ERRI-KEAAEKGLLYLGMGVSGGEEGARNGP-SL 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1815996340 141 MAGGDRDAFLAVEPIFNLL------GTNIVYQGNAGAGQHTKM 177
Cdd:PLN02350  147 MPGGSFEAYKNIEDILEKVaaqvddGPCVTYIGPGGAGNFVKM 189
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 9-177 6.77e-10

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 59.42  E-value: 6.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   9 IGFVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWA----------ETPAAVAKKANVIITIVGYPAdVEE 78
Cdd:PTZ00142    4 IGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEEFVKKAKEGNtrvkgyhtleELVNSLKKPRKVILLIKAGEA-VDE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  79 V------YLGENGIITNGRENTYvidmtTSTPTLAKRIYEEarkiGIYAIDAPVSGGDIGARDAKlSIMAGGDRDAFLAV 152
Cdd:PTZ00142   83 TidnllpLLEKGDIIIDGGNEWY-----LNTERRIKRCEEK----GILYLGMGVSGGEEGARYGP-SLMPGGNKEAYDHV 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1815996340 153 EPIFNLLGTNI------VYQGNAGAGQHTKM 177
Cdd:PTZ00142  153 KDILEKCSAKVgdspcvTYVGPGSSGHYVKM 183
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 9-79 1.34e-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: 57.38  E-value: 1.34e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1815996340   9 IGFVGTGVMGKSMAGHLLKAGYP---LVVYTRTKEKASELIEK-GAEWAETPAAVAKKANVIITIVGyPADVEEV 79
Cdd:COG0345     5 IGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSPERLEALAERyGVRVTTDNAEAAAQADVVVLAVK-PQDLAEV 78
PRK09287 PRK09287
NADP-dependent phosphogluconate dehydrogenase;
17-177 5.78e-09

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236453 [Multi-domain]  Cd Length: 459  Bit Score: 56.29  E-value: 5.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  17 MGKSMAGHLLKAGYPLVVYTRTKEKASELIE--------KGAEWAETPAAVAKKANVIITIV--GYPAD--VEEV--YLG 82
Cdd:PRK09287    1 MGKNLALNIASHGYTVAVYNRTPEKTDEFLAeegkgkkiVPAYTLEEFVASLEKPRKILLMVkaGAPVDavIEQLlpLLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  83 ENGIITNGrENTYVIDmtTStptlakRIYEEARKIGIYAIDAPVSGGDIGARDAKlSIMAGGDRDAFLAVEPIFnllgTN 162
Cdd:PRK09287   81 KGDIIIDG-GNSNYKD--TI------RREKELAEKGIHFIGMGVSGGEEGALHGP-SIMPGGQKEAYELVAPIL----EK 146

                         170       180
                  ....*....|....*....|....*.
gi 1815996340 163 I-----------VYQGNAGAGQHTKM 177
Cdd:PRK09287  147 IaakvedgepcvTYIGPDGAGHYVKM 172
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
9-67 3.06e-07

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


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 49.78  E-value: 3.06e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1815996340   9 IGFVGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWAE--TPAAVAKKANVII 67
Cdd:COG2085     1 IGIIGTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAELGPGARagTNAEAAAAADVVV 61
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 5-79 6.32e-07

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 49.76  E-value: 6.32e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1815996340   5 ENTVIGFVGTGVMGKSMAGHLLKAGYP---LVVYTRTKEKASELIEK-GAEWAETPAAVAKKANVIITIVGyPADVEEV 79
Cdd:PRK11880    1 MMKKIGFIGGGNMASAIIGGLLASGVPakdIIVSDPSPEKRAALAEEyGVRAATDNQEAAQEADVVVLAVK-PQVMEEV 78
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 9-67 1.20e-06

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


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 49.04  E-value: 1.20e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1815996340   9 IGFVGTGVMGKSMAGHLLKAGYPLV-VYTRTKEKASELIEK-GAEWAETPAAVAKKANVII 67
Cdd:COG5495     6 IGIIGAGRVGTALAAALRAAGHEVVgVYSRSPASAERAAALlGAVPALDLEELAAEADLVL 66
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 7-61 1.20e-04

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 42.14  E-value: 1.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1815996340   7 TVIGfvGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAEWAE----TPAAVAK 61
Cdd:COG0702     3 LVTG--ATGFIGRRVVRALLARGHPVRALVRDPEKAAALAAAGVEVVQgdldDPESLAA 59
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 7-78 3.64e-04

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 41.51  E-value: 3.64e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1815996340   7 TVIGfvGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEK-GAEWAETPAAVAKKANVIITIVgyPADVEE 78
Cdd:PRK08655    4 SIIG--GTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKElGVEYANDNIDAAKDADIVIISV--PINVTE 72
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
10-79 5.75e-04

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 38.37  E-value: 5.75e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1815996340  10 GFVGTGVMGKSMAGHLLKAGYP--LVVYTRTKEKASEL---IEKGAEwAETPAAVAKKANVIITIVGyPADVEEV 79
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGPHevVVANSRNPEKAEELaeeYGVGAT-AVDNEEAAEEADVVFLAVK-PEDAPDV 73
NmrA_TMR_like_1_SDR_a cd05231
NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, ...
 8-51 6.12e-04

NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, subgroup 1, atypical (a) SDRs; Atypical SDRs related to NMRa, TMR, and HSCARG (an NADPH sensor). This subgroup resembles the SDRs and has a partially conserved characteristic [ST]GXXGXXG NAD-binding motif, but lacks the conserved active site residues. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. 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. Atypical SDRs are distinct from classical SDRs. 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: 187542 [Multi-domain]  Cd Length: 259  Bit Score: 40.39  E-value: 6.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1815996340   8 VIGfvGTGVMGKSMAGHLLKAGYPLVVYTRTKEKASELIEKGAE 51
Cdd:cd05231     3 VTG--ATGRIGSKVATTLLEAGRPVRALVRSDERAAALAARGAE 44
NmrA pfam05368
NmrA-like family; NmrA is a negative transcriptional regulator involved in the ...
 7-77 6.56e-04

NmrA-like family; NmrA is a negative transcriptional regulator involved in the post-translational modification of the transcription factor AreA. NmrA is part of a system controlling nitrogen metabolite repression in fungi. This family only contains a few sequences as iteration results in significant matches to other Rossmann fold families.


Pssm-ID: 398829 [Multi-domain]  Cd Length: 236  Bit Score: 40.40  E-value: 6.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   7 TVIGfvGTGVMGKSMAGHLLKAGYPLVVYTR--TKEKASELIEKGAEWA-------ETPAAVAKKANVIITIVGYPADVE 77
Cdd:pfam05368   2 LVFG--ATGQQGGSVVRASLKAGHKVRALVRdpKSELAKSLKEAGVELVkgdlddkESLVEALKGVDVVFSVTGFWAGKE 79
PRK07680 PRK07680
late competence protein ComER; Validated
 9-66 2.24e-03

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 38.80  E-value: 2.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1815996340   9 IGFVGTGVMGKSMAGHLLKAGY----PLVVYTRTKEKASELIEK--GAEWAETPAAVAKKANVI 66
Cdd:PRK07680    3 IGFIGTGNMGTILIEAFLESGAvkpsQLTITNRTPAKAYHIKERypGIHVAKTIEEVISQSDLI 66
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 12-123 2.93e-03

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 37.64  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  12 VGTGVMGKSMAGHLLKAGYP-LVVYTRTKEKASELIEKGAEWAETPAAV-----AKKANVII--TIVGYpADVEEVYLGE 83
Cdd:cd01065    25 LGAGGAARAVAYALAELGAAkIVIVNRTLEKAKALAERFGELGIAIAYLdleelLAEADLIIntTPVGM-KPGDELPLPP 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1815996340  84 NGIitngRENTYVIDM-TTSTPTlakRIYEEARKIGIYAID 123
Cdd:cd01065   104 SLL----KPGGVVYDVvYNPLET---PLLKEARALGAKTID 137
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 13-66 5.53e-03

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 37.57  E-value: 5.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1815996340  13 GTGVMGKSMAGHLLKAGYPLVVYTRTKEKAS----ELIEKGAEwaetpaAVAKKANVI 66
Cdd:PRK08277   18 GGGVLGGAMAKELARAGAKVAILDRNQEKAEavvaEIKAAGGE------ALAVKADVL 69
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 11-79 6.68e-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: 37.78  E-value: 6.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340  11 FVGTGVMGKSMAGHLLKAGYP-LVVYTRTKEKASELIEK-GAE---WAETPAAVAkKANVIIT-------IVGyPADVEE 78
Cdd:COG0373   187 VIGAGEMGELAARHLAAKGVKrITVANRTLERAEELAEEfGGEavpLEELPEALA-EADIVISstgaphpVIT-KEMVER 264


                  .
gi 1815996340  79 V 79
Cdd:COG0373   265 A 265
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 9-88 9.51e-03

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: 37.03  E-value: 9.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815996340   9 IGFVGTGVMGKSMAGHLLKAGYPL--VVYTRTKEKASELIEKGA--EWAETPAAVAKKANVII--TIVGYPADV-EEV-- 79
Cdd:COG0287     4 IAIIGLGLIGGSLALALKRAGLAHevVGVDRSPETLERALELGVidRAATDLEEAVADADLVVlaVPVGATIEVlAELap 83


                  ....*....
gi 1815996340  80 YLGENGIIT 88
Cdd:COG0287    84 HLKPGAIVT 92
 
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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