SERC_METBF
ID SERC_METBF Reviewed; 370 AA.
AC P52878; Q46CY5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Phosphoserine aminotransferase;
DE EC=2.6.1.52;
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
DE Short=PSAT;
GN Name=serC; OrderedLocusNames=Mbar_A1294;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A PHOSPHOSERINE
RP AMINOTRANSFERASE, AND IDENTIFICATION OF THE TRANSCRIPTIONAL START SITE.
RX PubMed=8824630; DOI=10.1128/jb.178.19.5797-5802.1996;
RA Metcalf W.W., Zhang J.-K., Shi X., Wolfe R.S.;
RT "Molecular, genetic, and biochemical characterization of the serC gene of
RT Methanosarcina barkeri Fusaro.";
RL J. Bacteriol. 178:5797-5802(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
CC -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC phosphonooxybutanoate to phosphohydroxythreonine.
CC {ECO:0000269|PubMed:8824630}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate +
CC L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2-
CC oxo-4-phosphooxybutanoate + L-glutamate; Xref=Rhea:RHEA:16573,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58452,
CC ChEBI:CHEBI:58538; EC=2.6.1.52;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 2/3.
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily. {ECO:0000305}.
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DR EMBL; U51905; AAC44430.1; -; Genomic_DNA.
DR EMBL; CP000099; AAZ70257.1; -; Genomic_DNA.
DR RefSeq; WP_011306304.1; NC_007355.1.
DR AlphaFoldDB; P52878; -.
DR SMR; P52878; -.
DR STRING; 269797.Mbar_A1294; -.
DR PRIDE; P52878; -.
DR EnsemblBacteria; AAZ70257; AAZ70257; Mbar_A1294.
DR GeneID; 3627703; -.
DR KEGG; mba:Mbar_A1294; -.
DR eggNOG; arCOG00083; Archaea.
DR HOGENOM; CLU_040283_0_0_2; -.
DR OMA; TAFWDIA; -.
DR OrthoDB; 17822at2157; -.
DR BRENDA; 2.6.1.52; 3250.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00160; SerC_aminotrans_5; 1.
DR InterPro; IPR022278; Pser_aminoTfrase.
DR InterPro; IPR006271; Pser_aminoTfrase_methanosarc.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PIRSF; PIRSF000525; SerC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01365; serC_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aminotransferase; Cytoplasm; Pyridoxal phosphate;
KW Pyridoxine biosynthesis; Serine biosynthesis; Transferase.
FT CHAIN 1..370
FT /note="Phosphoserine aminotransferase"
FT /id="PRO_0000150230"
FT BINDING 38
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 243..244
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 190
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 370 AA; 41544 MW; 31B3963D12E28544 CRC64;
MKPTRVPNNP CFSSGPCAKH PGYSIEELKD TPFGRSHRSN LGKEKLAEAI KKTRDMLGLP
DDYLVGIVPA SDTGAFEMCL WSMLGCRGVD VLVWESFSKG WATDITKQLK LKDVRVFEAE
YGKLPDLKKV DFKNDVVFVW NGTTSGVKVP NGDWIPENRE GLTLCDATSA IFAMDIPYHK
LDVITFSWQK VLGGEGAHGM LILSPRAVQR LESYTPAWPL PKIFRLTKGG KLNKKIFEGS
TINTPSMLAN EDWLATLKWA ESVGGLKPLI QRTNDNLAVF EAFVAKNNWI HFLAETKEIR
SSTSVCFKVD LSDEKLKELI KTLEKEKVAY DIGSYRDAPS GLRIWCGATV EKEDLQCLCE
WIEWAYNLVK
