MULTISPECIES: homoserine dehydrogenase [Pseudomonas]
Protein Classification
homoserine dehydrogenase( domain architecture ID 11482218)
homoserine dehydrogenase catalyzes the conversion from L-homoserine and NAD(P)(+) to L-aspartate 4-semialdehyde and NAD(P)H
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| PRK06349 | PRK06349 | homoserine dehydrogenase; Provisional |
1-431 | 0e+00 | |||||||
homoserine dehydrogenase; Provisional : Pssm-ID: 235783 [Multi-domain] Cd Length: 426 Bit Score: 705.68 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||
| PRK06349 | PRK06349 | homoserine dehydrogenase; Provisional |
1-431 | 0e+00 | |||||||
homoserine dehydrogenase; Provisional Pssm-ID: 235783 [Multi-domain] Cd Length: 426 Bit Score: 705.68 E-value: 0e+00
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| ThrA | COG0460 | Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ... |
23-322 | 3.01e-164 | |||||||
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is part of the Pathway/BioSystem: Methionine biosynthesis Pssm-ID: 440228 [Multi-domain] Cd Length: 302 Bit Score: 463.75 E-value: 3.01e-164
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| Homoserine_dh | pfam00742 | Homoserine dehydrogenase; |
135-312 | 1.69e-93 | |||||||
Homoserine dehydrogenase; Pssm-ID: 459921 [Multi-domain] Cd Length: 178 Bit Score: 279.26 E-value: 1.69e-93
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| ACT_HSDH-Hom | cd04881 | ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine ... |
352-431 | 1.57e-27 | |||||||
ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) and related domains; The ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) encoded by the hom gene of Bacillus subtilis and other related sequences. HSDH reduces aspartate semi-aldehyde to the amino acid homoserine, one that is required for the biosynthesis of Met, Thr, and Ile from Asp. Neither the enzyme nor the aspartate pathway is found in the animal kingdom. This mostly bacterial HSDH group has a C-terminal ACT domain and is believed to be involved in enzyme regulation. A C-terminal deletion in the Corynebacterium glutamicum HSDH abolished allosteric inhibition by L-threonine. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153153 [Multi-domain] Cd Length: 79 Bit Score: 104.52 E-value: 1.57e-27
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| Name | Accession | Description | Interval | E-value | |||||||
| PRK06349 | PRK06349 | homoserine dehydrogenase; Provisional |
1-431 | 0e+00 | |||||||
homoserine dehydrogenase; Provisional Pssm-ID: 235783 [Multi-domain] Cd Length: 426 Bit Score: 705.68 E-value: 0e+00
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| ThrA | COG0460 | Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ... |
23-322 | 3.01e-164 | |||||||
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is part of the Pathway/BioSystem: Methionine biosynthesis Pssm-ID: 440228 [Multi-domain] Cd Length: 302 Bit Score: 463.75 E-value: 3.01e-164
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| Homoserine_dh | pfam00742 | Homoserine dehydrogenase; |
135-312 | 1.69e-93 | |||||||
Homoserine dehydrogenase; Pssm-ID: 459921 [Multi-domain] Cd Length: 178 Bit Score: 279.26 E-value: 1.69e-93
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| PRK06270 | PRK06270 | homoserine dehydrogenase; Provisional |
4-319 | 1.07e-83 | |||||||
homoserine dehydrogenase; Provisional Pssm-ID: 235763 [Multi-domain] Cd Length: 341 Bit Score: 260.18 E-value: 1.07e-83
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| PRK08374 | PRK08374 | homoserine dehydrogenase; Provisional |
4-313 | 7.13e-51 | |||||||
homoserine dehydrogenase; Provisional Pssm-ID: 169409 [Multi-domain] Cd Length: 336 Bit Score: 174.99 E-value: 7.13e-51
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| ACT_HSDH-Hom | cd04881 | ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine ... |
352-431 | 1.57e-27 | |||||||
ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) and related domains; The ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) encoded by the hom gene of Bacillus subtilis and other related sequences. HSDH reduces aspartate semi-aldehyde to the amino acid homoserine, one that is required for the biosynthesis of Met, Thr, and Ile from Asp. Neither the enzyme nor the aspartate pathway is found in the animal kingdom. This mostly bacterial HSDH group has a C-terminal ACT domain and is believed to be involved in enzyme regulation. A C-terminal deletion in the Corynebacterium glutamicum HSDH abolished allosteric inhibition by L-threonine. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153153 [Multi-domain] Cd Length: 79 Bit Score: 104.52 E-value: 1.57e-27
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| PRK06813 | PRK06813 | homoserine dehydrogenase; Validated |
84-317 | 1.34e-26 | |||||||
homoserine dehydrogenase; Validated Pssm-ID: 168683 [Multi-domain] Cd Length: 346 Bit Score: 109.57 E-value: 1.34e-26
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| PRK06392 | PRK06392 | homoserine dehydrogenase; Provisional |
4-226 | 8.29e-24 | |||||||
homoserine dehydrogenase; Provisional Pssm-ID: 102354 [Multi-domain] Cd Length: 326 Bit Score: 101.10 E-value: 8.29e-24
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| NAD_binding_3 | pfam03447 | Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ... |
10-127 | 4.22e-22 | |||||||
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model. Pssm-ID: 281446 [Multi-domain] Cd Length: 116 Bit Score: 90.83 E-value: 4.22e-22
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| thrA | PRK09436 | bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional |
6-312 | 1.26e-17 | |||||||
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional Pssm-ID: 181856 [Multi-domain] Cd Length: 819 Bit Score: 85.59 E-value: 1.26e-17
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| COG4091 | COG4091 | Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ... |
2-185 | 1.03e-11 | |||||||
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and metabolism]; Pssm-ID: 443267 [Multi-domain] Cd Length: 429 Bit Score: 66.33 E-value: 1.03e-11
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| PLN02700 | PLN02700 | homoserine dehydrogenase family protein |
126-315 | 7.80e-11 | |||||||
homoserine dehydrogenase family protein Pssm-ID: 215377 [Multi-domain] Cd Length: 377 Bit Score: 63.25 E-value: 7.80e-11
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| ACT | pfam01842 | ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ... |
352-417 | 3.01e-10 | |||||||
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5 Pssm-ID: 426468 [Multi-domain] Cd Length: 66 Bit Score: 55.78 E-value: 3.01e-10
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| SpoT | COG0317 | (p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription]; |
354-429 | 7.72e-08 | |||||||
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription]; Pssm-ID: 440086 [Multi-domain] Cd Length: 722 Bit Score: 54.78 E-value: 7.72e-08
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| metL | PRK09466 | bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional |
2-208 | 1.58e-07 | |||||||
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional Pssm-ID: 236530 [Multi-domain] Cd Length: 810 Bit Score: 53.77 E-value: 1.58e-07
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| ACT | cd02116 | ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
354-416 | 1.49e-06 | |||||||
ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times. Pssm-ID: 153139 [Multi-domain] Cd Length: 60 Bit Score: 45.36 E-value: 1.49e-06
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| MviM | COG0673 | Predicted dehydrogenase [General function prediction only]; |
1-125 | 3.08e-06 | |||||||
Predicted dehydrogenase [General function prediction only]; Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 48.77 E-value: 3.08e-06
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| GcvR | COG2716 | Glycine cleavage system regulator GcvR [Amino acid transport and metabolism]; |
352-418 | 1.10e-05 | |||||||
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism]; Pssm-ID: 442029 [Multi-domain] Cd Length: 174 Bit Score: 45.60 E-value: 1.10e-05
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| ACT_RelA-SpoT | cd04876 | ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found ... |
354-422 | 1.37e-05 | |||||||
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found C-terminal of the RelA/SpoT domains. Enzymes of the Rel/Spo family enable bacteria to survive prolonged periods of nutrient limitation by controlling guanosine-3'-diphosphate-5'-(tri)diphosphate ((p)ppGpp) production and subsequent rRNA repression (stringent response). Both the synthesis of (p)ppGpp from ATP and GDP(GTP), and its hydrolysis to GDP(GTP) and pyrophosphate, are catalyzed by Rel/Spo proteins. In Escherichia coli and its close relatives, the metabolism of (p)ppGpp is governed by two homologous proteins, RelA and SpoT. The RelA protein catalyzes (p)ppGpp synthesis in a reaction requiring its binding to ribosomes bearing codon-specified uncharged tRNA. The major role of the SpoT protein is the breakdown of (p)ppGpp by a manganese-dependent (p)ppGpp pyrophosphohydrolase activity. Although the stringent response appears to be tightly regulated by these two enzymes in E. coli, a bifunctional Rel/Spo protein has been discovered in most gram-positive organisms studied so far. These bifunctional Rel/Spo homologs (rsh) appear to modulate (p)ppGpp levels through two distinct active sites that are controlled by a reciprocal regulatory mechanism ensuring inverse coupling of opposing activities. In studies with the Streptococcus equisimilis Rel/Spo homolog, the C-terminal domain appears to be involved in this reciprocal regulation of the two opposing catalytic activities present in the N-terminal domain, ensuring that both synthesis and degradation activities are not coinduced. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153148 [Multi-domain] Cd Length: 71 Bit Score: 42.82 E-value: 1.37e-05
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| ACT_AHAS | cd04878 | N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid ... |
359-391 | 3.24e-05 | |||||||
N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid synthase (AHAS); ACT_AHAS: N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid synthase (AHAS). AHAS catalyses the first common step in the biosynthesis of the three branched-chain amino acids. The first step involves the condensation of either pyruvate or 2-ketobutyrate with the two-carbon hydroxyethyl fragment derived from another pyruvate molecule, covalently bound to the coenzyme thiamine diphosphate. Bacterial AHASs generally consist of regulatory and catalytic subunits. The effector (valine) binding sites are proposed to be located in two symmetrically related positions in the interface between a pair of N-terminal ACT domains with the C-terminal domain of IlvH contacting the catalytic dimer. Plants Arabidopsis and Oryza have tandem IlvH subunits; both the first and second ACT domain sequences are present in this CD. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153150 Cd Length: 72 Bit Score: 41.73 E-value: 3.24e-05
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| GFO_IDH_MocA | pfam01408 | Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ... |
4-124 | 3.74e-04 | |||||||
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot. Pssm-ID: 426248 [Multi-domain] Cd Length: 120 Bit Score: 39.88 E-value: 3.74e-04
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| IlvH | COG0440 | Acetolactate synthase, small subunit [Amino acid transport and metabolism]; Acetolactate ... |
360-382 | 4.68e-04 | |||||||
Acetolactate synthase, small subunit [Amino acid transport and metabolism]; Acetolactate synthase, small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis Pssm-ID: 440209 [Multi-domain] Cd Length: 160 Bit Score: 40.39 E-value: 4.68e-04
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| ACT_4 | pfam13291 | ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ... |
354-421 | 6.77e-04 | |||||||
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT domains are found at the C-terminus of the RelA protein. Pssm-ID: 463831 [Multi-domain] Cd Length: 79 Bit Score: 38.31 E-value: 6.77e-04
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| ACT_3PGDH-like | cd04879 | ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate ... |
356-422 | 1.13e-03 | |||||||
ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH); ACT_3PGDH-like: The ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH), with or without an extended C-terminal (xct) region found in various bacteria, archaea, fungi, and plants. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In bacteria, 3PGDH is feedback controlled by the end product L-serine in an allosteric manner. In the Escherichia coli homotetrameric enzyme, the interface at adjacent ACT (regulatory) domains couples to create an extended beta-sheet. Each regulatory interface forms two serine-binding sites. The mechanism by which serine transmits inhibition to the active site is postulated to involve the tethering of the regulatory domains together to create a rigid quaternary structure with a solvent-exposed active site cleft. This CD also includes the C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillus, and Treponema species. LSD enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in E. coli, and other Enterobacteriales, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153151 Cd Length: 71 Bit Score: 37.44 E-value: 1.13e-03
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| ACT_LSD | cd04903 | C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit; ... |
354-422 | 1.54e-03 | |||||||
C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit; The C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillis, and Treponema species. These enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in Escherichia coli, and other enterobacterials, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153175 Cd Length: 71 Bit Score: 37.13 E-value: 1.54e-03
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| nat-AmDH_N_like | cd24146 | N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ... |
4-124 | 3.39e-03 | |||||||
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain. Pssm-ID: 467616 [Multi-domain] Cd Length: 157 Bit Score: 37.91 E-value: 3.39e-03
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| ACT_AcuB | cd04883 | C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB; This CD ... |
354-382 | 3.69e-03 | |||||||
C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB; This CD includes the C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB. AcuB is putatively involved in the anaerobic catabolism of acetoin, and related proteins. Studies report the induction of AcuB by nitrate respiration and also by fermentation. Since acetoin can be secreted and later serve as a source of carbon, it has been proposed that, during anaerobic growth when other carbon sources are exhausted, the induction of the AcuB protein results in acetoin catabolism. AcuB-like proteins have two N-terminal tandem CBS domains and a single C-terminal ACT domain. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153155 Cd Length: 72 Bit Score: 36.08 E-value: 3.69e-03
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| PRK08577 | PRK08577 | hypothetical protein; Provisional |
342-379 | 6.32e-03 | |||||||
hypothetical protein; Provisional Pssm-ID: 236301 [Multi-domain] Cd Length: 136 Bit Score: 36.90 E-value: 6.32e-03
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| ACT_Bt0572_2 | cd04882 | C-terminal ACT domain of a novel protein composed of just two ACT domains; Included in this CD ... |
354-382 | 7.54e-03 | |||||||
C-terminal ACT domain of a novel protein composed of just two ACT domains; Included in this CD is the C-terminal ACT domain of a novel protein composed of just two ACT domains, as seen in the yet uncharacterized structure (pdb 2F06) of the Bt0572 protein from Bacteroides thetaiotaomicron and related proteins. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153154 Cd Length: 65 Bit Score: 34.89 E-value: 7.54e-03
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| ACT_Af1403 | cd04874 | N-terminal ACT domain of the yet uncharacterized, small (~133 a.a.), putative amino acid ... |
354-384 | 8.08e-03 | |||||||
N-terminal ACT domain of the yet uncharacterized, small (~133 a.a.), putative amino acid binding protein, Af1403, and related domains; This CD includes the N-terminal ACT domain of the yet uncharacterized, small (~133 a.a.), putative amino acid binding protein, Af1403, from Archaeoglobus fulgidus and other related archeal ACT domains. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153146 [Multi-domain] Cd Length: 72 Bit Score: 34.97 E-value: 8.08e-03
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