Ahcyl1 protein [Danio rerio]
Protein Classification
adenosylhomocysteinase family protein( domain architecture ID 11278876)
adenosylhomocysteinase family protein such as adenosylhomocysteinase that catalyzes the hydrolysis of S-adenosyl-L-homocysteine to form L-homocysteine and adenosine and may play a key role in regulating the intracellular concentration of adenosylhomocysteine
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| AdoHcyase | smart00996 | S-adenosyl-L-homocysteine hydrolase; |
88-511 | 0e+00 | |||||||
S-adenosyl-L-homocysteine hydrolase; : Pssm-ID: 214963 [Multi-domain] Cd Length: 426 Bit Score: 871.09 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||
| AdoHcyase | smart00996 | S-adenosyl-L-homocysteine hydrolase; |
88-511 | 0e+00 | |||||||
S-adenosyl-L-homocysteine hydrolase; Pssm-ID: 214963 [Multi-domain] Cd Length: 426 Bit Score: 871.09 E-value: 0e+00
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| AdoHcyase | pfam05221 | S-adenosyl-L-homocysteine hydrolase; |
86-511 | 0e+00 | |||||||
S-adenosyl-L-homocysteine hydrolase; Pssm-ID: 461594 Cd Length: 429 Bit Score: 827.08 E-value: 0e+00
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| SAHH | cd00401 | S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ... |
96-500 | 0e+00 | |||||||
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+. Pssm-ID: 240619 [Multi-domain] Cd Length: 402 Bit Score: 753.14 E-value: 0e+00
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| PRK05476 | PRK05476 | S-adenosyl-L-homocysteine hydrolase; Provisional |
86-506 | 0e+00 | |||||||
S-adenosyl-L-homocysteine hydrolase; Provisional Pssm-ID: 235488 [Multi-domain] Cd Length: 425 Bit Score: 681.85 E-value: 0e+00
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| SAM1 | COG0499 | S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism]; |
86-504 | 0e+00 | |||||||
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism]; Pssm-ID: 440265 [Multi-domain] Cd Length: 420 Bit Score: 673.30 E-value: 0e+00
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| ahcY | TIGR00936 | adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ... |
96-504 | 0e+00 | |||||||
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the regeneration of the methyl donor S-adenosylmethionine. Species that lack this enzyme are likely to have adenosylhomocysteine nucleosidase (EC 3.2.2.9), an enzyme which also acts as 5'-methyladenosine nucleosidase (see TIGR01704). [Energy metabolism, Amino acids and amines] Pssm-ID: 213572 Cd Length: 407 Bit Score: 526.20 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||
| AdoHcyase | smart00996 | S-adenosyl-L-homocysteine hydrolase; |
88-511 | 0e+00 | |||||||
S-adenosyl-L-homocysteine hydrolase; Pssm-ID: 214963 [Multi-domain] Cd Length: 426 Bit Score: 871.09 E-value: 0e+00
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| AdoHcyase | pfam05221 | S-adenosyl-L-homocysteine hydrolase; |
86-511 | 0e+00 | |||||||
S-adenosyl-L-homocysteine hydrolase; Pssm-ID: 461594 Cd Length: 429 Bit Score: 827.08 E-value: 0e+00
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| SAHH | cd00401 | S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ... |
96-500 | 0e+00 | |||||||
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+. Pssm-ID: 240619 [Multi-domain] Cd Length: 402 Bit Score: 753.14 E-value: 0e+00
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| PRK05476 | PRK05476 | S-adenosyl-L-homocysteine hydrolase; Provisional |
86-506 | 0e+00 | |||||||
S-adenosyl-L-homocysteine hydrolase; Provisional Pssm-ID: 235488 [Multi-domain] Cd Length: 425 Bit Score: 681.85 E-value: 0e+00
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| SAM1 | COG0499 | S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism]; |
86-504 | 0e+00 | |||||||
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism]; Pssm-ID: 440265 [Multi-domain] Cd Length: 420 Bit Score: 673.30 E-value: 0e+00
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| PTZ00075 | PTZ00075 | Adenosylhomocysteinase; Provisional |
85-512 | 0e+00 | |||||||
Adenosylhomocysteinase; Provisional Pssm-ID: 240258 Cd Length: 476 Bit Score: 600.87 E-value: 0e+00
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| ahcY | TIGR00936 | adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ... |
96-504 | 0e+00 | |||||||
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the regeneration of the methyl donor S-adenosylmethionine. Species that lack this enzyme are likely to have adenosylhomocysteine nucleosidase (EC 3.2.2.9), an enzyme which also acts as 5'-methyladenosine nucleosidase (see TIGR01704). [Energy metabolism, Amino acids and amines] Pssm-ID: 213572 Cd Length: 407 Bit Score: 526.20 E-value: 0e+00
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| PLN02494 | PLN02494 | adenosylhomocysteinase |
86-512 | 2.83e-179 | |||||||
adenosylhomocysteinase Pssm-ID: 178111 [Multi-domain] Cd Length: 477 Bit Score: 512.10 E-value: 2.83e-179
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| AdoHcyase_NAD | pfam00670 | S-adenosyl-L-homocysteine hydrolase, NAD binding domain; |
271-431 | 1.83e-104 | |||||||
S-adenosyl-L-homocysteine hydrolase, NAD binding domain; Pssm-ID: 395543 [Multi-domain] Cd Length: 162 Bit Score: 309.28 E-value: 1.83e-104
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| AdoHcyase_NAD | smart00997 | S-adenosyl-L-homocysteine hydrolase, NAD binding domain; |
271-432 | 2.39e-104 | |||||||
S-adenosyl-L-homocysteine hydrolase, NAD binding domain; Pssm-ID: 198065 [Multi-domain] Cd Length: 162 Bit Score: 309.00 E-value: 2.39e-104
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| FDH_GDH_like | cd12154 | Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ... |
130-451 | 1.02e-44 | |||||||
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related dehydrogenases; The formate/glycerate dehydrogenase like family contains a diverse group of enzymes such as formate dehydrogenase (FDH), glycerate dehydrogenase (GDH), D-lactate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine hydrolase, that share a common 2-domain structure. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar domains of the alpha/beta Rossmann fold NAD+ binding form. The NAD(P) binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD(P) is bound, primarily to the C-terminal portion of the 2nd (internal) domain. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of a hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. Pssm-ID: 240631 [Multi-domain] Cd Length: 310 Bit Score: 159.70 E-value: 1.02e-44
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| TrkA | COG0569 | Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
294-412 | 1.57e-08 | |||||||
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: 56.23 E-value: 1.57e-08
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| AlaDh_PNT_C | smart01002 | Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
296-389 | 3.85e-08 | |||||||
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine. Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 52.51 E-value: 3.85e-08
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| DpaA | COG5842 | Dipicolinate synthase subunit A (sporulation protein SpoVFA) [Cell cycle control, cell ... |
293-390 | 1.28e-06 | |||||||
Dipicolinate synthase subunit A (sporulation protein SpoVFA) [Cell cycle control, cell division, chromosome partitioning, Amino acid transport and metabolism]; Pssm-ID: 444544 [Multi-domain] Cd Length: 288 Bit Score: 50.15 E-value: 1.28e-06
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| 2-Hacid_dh_1 | cd05300 | Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ... |
293-380 | 1.09e-04 | |||||||
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomains but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Pssm-ID: 240625 [Multi-domain] Cd Length: 313 Bit Score: 44.43 E-value: 1.09e-04
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| AlaDh_PNT_C | pfam01262 | Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
296-389 | 2.88e-04 | |||||||
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases. Pssm-ID: 426165 [Multi-domain] Cd Length: 213 Bit Score: 42.10 E-value: 2.88e-04
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| 2-Hacid_dh_C | pfam02826 | D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ... |
293-380 | 6.56e-04 | |||||||
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389. Pssm-ID: 427007 [Multi-domain] Cd Length: 178 Bit Score: 40.56 E-value: 6.56e-04
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| NAD_bind_Glutamyl_tRNA_reduct | cd05213 | NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ... |
277-357 | 6.59e-04 | |||||||
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (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 DH, 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: 133452 [Multi-domain] Cd Length: 311 Bit Score: 41.87 E-value: 6.59e-04
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| L-AlaDH | cd05305 | Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
296-389 | 9.45e-04 | |||||||
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms. Pssm-ID: 240630 [Multi-domain] Cd Length: 359 Bit Score: 41.62 E-value: 9.45e-04
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| TrkA_N | pfam02254 | TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ... |
296-409 | 1.06e-03 | |||||||
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: 39.05 E-value: 1.06e-03
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| PRK08306 | PRK08306 | dipicolinate synthase subunit DpsA; |
287-390 | 1.21e-03 | |||||||
dipicolinate synthase subunit DpsA; Pssm-ID: 181371 [Multi-domain] Cd Length: 296 Bit Score: 40.98 E-value: 1.21e-03
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| formate_dh_like | cd05198 | Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ... |
293-378 | 1.65e-03 | |||||||
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Pssm-ID: 240622 [Multi-domain] Cd Length: 302 Bit Score: 40.69 E-value: 1.65e-03
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| PGDH_like_3 | cd12174 | Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ... |
293-379 | 2.40e-03 | |||||||
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric. Pssm-ID: 240651 [Multi-domain] Cd Length: 305 Bit Score: 39.85 E-value: 2.40e-03
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| 2-Hacid_dh_6 | cd12165 | Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ... |
289-380 | 5.38e-03 | |||||||
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Pssm-ID: 240642 [Multi-domain] Cd Length: 314 Bit Score: 39.15 E-value: 5.38e-03
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| 2-Hacid_dh_12 | cd12177 | Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ... |
291-378 | 5.56e-03 | |||||||
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Pssm-ID: 240654 [Multi-domain] Cd Length: 321 Bit Score: 38.84 E-value: 5.56e-03
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| PGDH_2 | cd05303 | Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ... |
293-379 | 7.54e-03 | |||||||
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate dehydrogenase (PGDH) catalyzes the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDH comes in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Pssm-ID: 240628 [Multi-domain] Cd Length: 301 Bit Score: 38.29 E-value: 7.54e-03
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