ID A1ALZ6_PELPD Unreviewed; 364 AA.
AC A1ALZ6;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Phosphoserine aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160};
DE EC=2.6.1.52 {ECO:0000256|HAMAP-Rule:MF_00160};
DE AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160};
DE Short=PSAT {ECO:0000256|HAMAP-Rule:MF_00160};
GN Name=serC {ECO:0000256|HAMAP-Rule:MF_00160};
GN OrderedLocusNames=Ppro_0735 {ECO:0000313|EMBL:ABK98366.1};
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK98366.1, ECO:0000313|Proteomes:UP000006732};
RN [1] {ECO:0000313|EMBL:ABK98366.1, ECO:0000313|Proteomes:UP000006732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1
RC {ECO:0000313|Proteomes:UP000006732};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC phosphonooxybutanoate to phosphohydroxythreonine. {ECO:0000256|HAMAP-
CC Rule:MF_00160}.
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 Evidence={ECO:0000256|ARBA:ARBA00001607, ECO:0000256|HAMAP-
CC Rule:MF_00160};
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 Evidence={ECO:0000256|ARBA:ARBA00001871, ECO:0000256|HAMAP-
CC Rule:MF_00160};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00160};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00160};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 2/3. {ECO:0000256|ARBA:ARBA00005099,
CC ECO:0000256|HAMAP-Rule:MF_00160}.
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
CC {ECO:0000256|HAMAP-Rule:MF_00160}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00160}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily.
CC {ECO:0000256|ARBA:ARBA00006904, ECO:0000256|HAMAP-Rule:MF_00160}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00160}.
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DR EMBL; CP000482; ABK98366.1; -; Genomic_DNA.
DR RefSeq; WP_011734678.1; NC_008609.1.
DR AlphaFoldDB; A1ALZ6; -.
DR STRING; 338966.Ppro_0735; -.
DR KEGG; ppd:Ppro_0735; -.
DR eggNOG; COG1932; Bacteria.
DR HOGENOM; CLU_034866_0_2_7; -.
DR OrthoDB; 9809412at2; -.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR Proteomes; UP000006732; Chromosome.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00160; SerC_aminotrans_5; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR022278; Pser_aminoTfrase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01364; serC_1; 1.
DR PANTHER; PTHR43247; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43247:SF1; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000525; SerC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00160};
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW Rule:MF_00160}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00160};
KW Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160};
KW Reference proteome {ECO:0000313|Proteomes:UP000006732};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299, ECO:0000256|HAMAP-
KW Rule:MF_00160};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00160, ECO:0000313|EMBL:ABK98366.1}.
FT DOMAIN 5..352
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 42
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT BINDING 76..77
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT BINDING 102
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT BINDING 150
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT BINDING 170
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT BINDING 193
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT BINDING 235..236
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT MOD_RES 194
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
SQ SEQUENCE 364 AA; 40060 MW; C5C3B683BDBFE048 CRC64;
MKRFYNFSAG PSMLPESVLA KAADEMLCYE TSGQSVMEMS HRSKPFEAII AGAEALVRQN
MAIPDDYHVL FLQGGASLQF HMLPLNFMTI NKKADFTLTG TWAQKAAEEA KRLGTANIVG
SSKDKKWSYL PEITGADPEA DYFHICYNNT IEGTQYHSIP EVGAVPLIGD ISSGVLSAPL
DVTRFAVLYA GAQKNLGPAG VTLVIIRKDM MERIPAGLPA MLSYKTHVDG GSMYNTPPCY
AIYIFKLVQE WIRDMGGAEV IYRQNQEKAR LLYDFLDSSS LFFSPVEKSV RSLMNVPFLT
TEKDADKAEA LNKKFVKESE AAGLVNLAGH RSVGGMRASI YNAMPLEGVQ ALVAFMKEFE
ARCA
//
