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Database: UniProt
Entry: A0A0N0AEL7_9ACTN
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ID   A0A0N0AEL7_9ACTN        Unreviewed;       344 AA.
AC   A0A0N0AEL7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=phosphoserine transaminase {ECO:0000256|ARBA:ARBA00013030};
DE            EC=2.6.1.52 {ECO:0000256|ARBA:ARBA00013030};
DE   AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000256|ARBA:ARBA00031421};
GN   ORFNames=ADL04_10110 {ECO:0000313|EMBL:KOX03614.1};
OS   Streptomyces sp. NRRL B-3648.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519493 {ECO:0000313|EMBL:KOX03614.1, ECO:0000313|Proteomes:UP000037702};
RN   [1] {ECO:0000313|EMBL:KOX03614.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-3648 {ECO:0000313|EMBL:KOX03614.1};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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};
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};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 2/3. {ECO:0000256|ARBA:ARBA00005099}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. SerC subfamily.
CC       {ECO:0000256|ARBA:ARBA00006904}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOX03614.1}.
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DR   EMBL; LGDZ01000107; KOX03614.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0AEL7; -.
DR   PATRIC; fig|1519493.3.peg.2159; -.
DR   UniPathway; UPA00135; UER00197.
DR   Proteomes; UP000037702; Unassembled WGS sequence.
DR   GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
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   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR022278; Pser_aminoTfrase.
DR   InterPro; IPR006272; Pser_aminoTfrase_mycobac.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01366; serC_3; 1.
DR   PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR   PANTHER; PTHR21152:SF24; SERINE--PYRUVATE 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};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:KOX03614.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037702};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW   Transferase {ECO:0000313|EMBL:KOX03614.1}.
FT   DOMAIN          13..303
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   344 AA;  36866 MW;  508621632BC420B5 CRC64;
     MDALAATGTS LLGTSHRQAP VKNLVGKVRE GISELFSLPE GYEVVLGNGG STAFWDIATH
     GLIENKSQHL NFGEFSSKFA KAAKLAPWLA EPTVIASDPG THPEPQAEAG VDVYAFTHNE
     TSTGVAMPIK RVAGADEGAL VLVDATSGAG GLPVDIAETD VYYFAPQKSF ASDGGLWIGV
     FSPAAIERAE RVHASGRHVP EFFSLPTAID NSRKNQTYNT PALATLFLLN EQLEWLNGQG
     GLAWSTARTK DSSTRLYGWA EEAKYATPFV TDPAKRSQVI GTIDFSDEID AAAVAKVLRA
     NGIVDTEPYR KLGRNQLRIA MFPAIDPADV EALTKCVDYV IEKL
//
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