Kef-type K+ transport systems (NAD-binding component fused to domain related to exopolyphosphatase) [Methanosarcina barkeri 3]
Protein Classification
DHH family phosphoesterase( domain architecture ID 12033305)
DHH family phosphoesterase with TrkA-N domain similar to Methanocaldococcus jannaschii uncharacterized protein MJ1633
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| NrnA | COG0618 | nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and ... |
175-454 | 2.54e-75 | |||||
nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and metabolism, Signal transduction mechanisms]; : Pssm-ID: 440383 [Multi-domain] Cd Length: 312 Bit Score: 239.71 E-value: 2.54e-75
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| TrkA_N | pfam02254 | TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ... |
37-153 | 8.57e-26 | |||||
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD. : Pssm-ID: 426679 [Multi-domain] Cd Length: 115 Bit Score: 101.45 E-value: 8.57e-26
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| Name | Accession | Description | Interval | E-value | |||||
| NrnA | COG0618 | nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and ... |
175-454 | 2.54e-75 | |||||
nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and metabolism, Signal transduction mechanisms]; Pssm-ID: 440383 [Multi-domain] Cd Length: 312 Bit Score: 239.71 E-value: 2.54e-75
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| TrkA_N | pfam02254 | TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ... |
37-153 | 8.57e-26 | |||||
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD. Pssm-ID: 426679 [Multi-domain] Cd Length: 115 Bit Score: 101.45 E-value: 8.57e-26
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| TrkA | COG0569 | Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
30-229 | 4.61e-21 | |||||
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms]; Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 93.59 E-value: 4.61e-21
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| DHH | pfam01368 | DHH family; It is predicted that this family of proteins all perform a phosphoesterase ... |
188-332 | 1.28e-13 | |||||
DHH family; It is predicted that this family of proteins all perform a phosphoesterase function. It included the single stranded DNA exonuclease RecJ. Pssm-ID: 460177 [Multi-domain] Cd Length: 145 Bit Score: 67.98 E-value: 1.28e-13
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| PRK05427 | PRK05427 | putative manganese-dependent inorganic pyrophosphatase; Provisional |
191-343 | 2.37e-08 | |||||
putative manganese-dependent inorganic pyrophosphatase; Provisional Pssm-ID: 235458 [Multi-domain] Cd Length: 308 Bit Score: 55.60 E-value: 2.37e-08
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| PRK10669 | PRK10669 | putative cation:proton antiport protein; Provisional |
38-169 | 1.68e-07 | |||||
putative cation:proton antiport protein; Provisional Pssm-ID: 182633 [Multi-domain] Cd Length: 558 Bit Score: 53.95 E-value: 1.68e-07
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| NmrA_TMR_like_1_SDR_a | cd05231 | NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, ... |
37-92 | 3.56e-05 | |||||
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: 45.40 E-value: 3.56e-05
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| Name | Accession | Description | Interval | E-value | |||||
| NrnA | COG0618 | nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and ... |
175-454 | 2.54e-75 | |||||
nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and metabolism, Signal transduction mechanisms]; Pssm-ID: 440383 [Multi-domain] Cd Length: 312 Bit Score: 239.71 E-value: 2.54e-75
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| TrkA_N | pfam02254 | TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ... |
37-153 | 8.57e-26 | |||||
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD. Pssm-ID: 426679 [Multi-domain] Cd Length: 115 Bit Score: 101.45 E-value: 8.57e-26
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| TrkA | COG0569 | Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
30-229 | 4.61e-21 | |||||
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms]; Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 93.59 E-value: 4.61e-21
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| Kch | COG1226 | Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism]; |
34-186 | 7.81e-20 | |||||
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism]; Pssm-ID: 440839 [Multi-domain] Cd Length: 279 Bit Score: 89.40 E-value: 7.81e-20
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| DHH | pfam01368 | DHH family; It is predicted that this family of proteins all perform a phosphoesterase ... |
188-332 | 1.28e-13 | |||||
DHH family; It is predicted that this family of proteins all perform a phosphoesterase function. It included the single stranded DNA exonuclease RecJ. Pssm-ID: 460177 [Multi-domain] Cd Length: 145 Bit Score: 67.98 E-value: 1.28e-13
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| PPX1 | COG1227 | Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion]; |
194-354 | 8.32e-12 | |||||
Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion]; Pssm-ID: 440840 [Multi-domain] Cd Length: 307 Bit Score: 65.95 E-value: 8.32e-12
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| PRK05427 | PRK05427 | putative manganese-dependent inorganic pyrophosphatase; Provisional |
191-343 | 2.37e-08 | |||||
putative manganese-dependent inorganic pyrophosphatase; Provisional Pssm-ID: 235458 [Multi-domain] Cd Length: 308 Bit Score: 55.60 E-value: 2.37e-08
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| PRK10669 | PRK10669 | putative cation:proton antiport protein; Provisional |
38-169 | 1.68e-07 | |||||
putative cation:proton antiport protein; Provisional Pssm-ID: 182633 [Multi-domain] Cd Length: 558 Bit Score: 53.95 E-value: 1.68e-07
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| DHHA1 | pfam02272 | DHHA1 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ... |
362-453 | 1.81e-06 | |||||
DHHA1 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called DHHA1 for DHH associated domain. This domain is diagnostic of DHH subfamily 1 members. This domains is also found in alanyl tRNA synthetase, suggesting that this domain may have an RNA binding function. The domain is about 60 residues long and contains a conserved GG motif. Pssm-ID: 396724 [Multi-domain] Cd Length: 139 Bit Score: 47.44 E-value: 1.81e-06
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| trkA | PRK09496 | Trk system potassium transporter TrkA; |
38-166 | 5.39e-06 | |||||
Trk system potassium transporter TrkA; Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 48.97 E-value: 5.39e-06
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| WcaG | COG0451 | Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis]; |
36-94 | 6.98e-06 | |||||
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440220 [Multi-domain] Cd Length: 295 Bit Score: 47.67 E-value: 6.98e-06
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| YbjT | COG0702 | Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ... |
36-122 | 1.51e-05 | |||||
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: 45.99 E-value: 1.51e-05
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| trkA | PRK09496 | Trk system potassium transporter TrkA; |
28-172 | 2.71e-05 | |||||
Trk system potassium transporter TrkA; Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 46.65 E-value: 2.71e-05
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| NmrA_TMR_like_1_SDR_a | cd05231 | NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, ... |
37-92 | 3.56e-05 | |||||
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: 45.40 E-value: 3.56e-05
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| SDR_c2 | cd05370 | classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ... |
41-93 | 2.01e-04 | |||||
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Pssm-ID: 187628 [Multi-domain] Cd Length: 228 Bit Score: 42.68 E-value: 2.01e-04
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| SDR_a5 | cd05243 | atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ... |
36-104 | 3.46e-04 | |||||
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one 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 very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. 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: 187554 [Multi-domain] Cd Length: 203 Bit Score: 41.84 E-value: 3.46e-04
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| PRK14538 | PRK14538 | putative bifunctional signaling protein/50S ribosomal protein L9; Provisional |
191-454 | 4.74e-04 | |||||
putative bifunctional signaling protein/50S ribosomal protein L9; Provisional Pssm-ID: 173004 [Multi-domain] Cd Length: 838 Bit Score: 42.89 E-value: 4.74e-04
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| adh_short | pfam00106 | short chain dehydrogenase; This family contains a wide variety of dehydrogenases. |
38-94 | 1.47e-03 | |||||
short chain dehydrogenase; This family contains a wide variety of dehydrogenases. Pssm-ID: 395056 [Multi-domain] Cd Length: 195 Bit Score: 39.90 E-value: 1.47e-03
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| DltE | COG3967 | Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ... |
38-101 | 1.67e-03 | |||||
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism]; Pssm-ID: 443167 [Multi-domain] Cd Length: 246 Bit Score: 40.15 E-value: 1.67e-03
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| PRK14869 | PRK14869 | putative manganese-dependent inorganic diphosphatase; |
280-354 | 2.06e-03 | |||||
putative manganese-dependent inorganic diphosphatase; Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 40.59 E-value: 2.06e-03
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| BKR_like_SDR_like | cd05344 | putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ... |
36-94 | 2.10e-03 | |||||
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs. Pssm-ID: 187602 [Multi-domain] Cd Length: 253 Bit Score: 39.95 E-value: 2.10e-03
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| PRK04148 | PRK04148 | hypothetical protein; Provisional |
45-90 | 3.34e-03 | |||||
hypothetical protein; Provisional Pssm-ID: 235226 Cd Length: 134 Bit Score: 37.68 E-value: 3.34e-03
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| YqjQ | COG0300 | Short-chain dehydrogenase [General function prediction only]; |
34-94 | 3.94e-03 | |||||
Short-chain dehydrogenase [General function prediction only]; Pssm-ID: 440069 [Multi-domain] Cd Length: 252 Bit Score: 39.08 E-value: 3.94e-03
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| PRK06940 | PRK06940 | short chain dehydrogenase; Provisional |
37-91 | 7.42e-03 | |||||
short chain dehydrogenase; Provisional Pssm-ID: 180766 [Multi-domain] Cd Length: 275 Bit Score: 38.46 E-value: 7.42e-03
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| SDR_e_a | cd05226 | Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ... |
38-123 | 8.01e-03 | |||||
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding 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. 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: 187537 [Multi-domain] Cd Length: 176 Bit Score: 37.38 E-value: 8.01e-03
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| Blast search parameters | ||||
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