ID A0A0U3PPE2_9MICC Unreviewed; 375 AA.
AC A0A0U3PPE2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Phosphoserine aminotransferase {ECO:0000256|ARBA:ARBA00021164};
DE EC=2.6.1.52 {ECO:0000256|ARBA:ARBA00013030};
DE AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000256|ARBA:ARBA00031421};
GN ORFNames=MB46_00980 {ECO:0000313|EMBL:ALV44296.1};
OS Arthrobacter alpinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=656366 {ECO:0000313|EMBL:ALV44296.1, ECO:0000313|Proteomes:UP000055883};
RN [1] {ECO:0000313|EMBL:ALV44296.1, ECO:0000313|Proteomes:UP000055883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3 {ECO:0000313|EMBL:ALV44296.1,
RC ECO:0000313|Proteomes:UP000055883};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-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}.
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DR EMBL; CP013745; ALV44296.1; -; Genomic_DNA.
DR RefSeq; WP_044576926.1; NZ_CP013745.1.
DR AlphaFoldDB; A0A0U3PPE2; -.
DR STRING; 656366.AS189_17895; -.
DR KEGG; arw:MB46_00980; -.
DR eggNOG; COG1932; Bacteria.
DR OrthoDB; 975012at2; -.
DR UniPathway; UPA00135; UER00197.
DR Proteomes; UP000055883; Chromosome.
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; 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};
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:ALV44296.1};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW Transferase {ECO:0000313|EMBL:ALV44296.1}.
FT DOMAIN 148..334
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 375 AA; 39639 MW; 94BD223184D4C0F8 CRC64;
MSESTPLTIP ANLLPADGRF GAGPSKVRAE QVAALSEAGA SLLGTSHRQA PIKNLVGDIR
TGLKEFFKAP EGYEVILGVG GSTAFWDVAT FGLVEKKAQH LSFGEFGSKF AAATNNAPFL
DASSIIKADP GTRPVAVAEA GVDAYAWPQN ETSTGVAAPV KRVAGADDGA LVLIDATSAA
GGLAVDVSES DVYYFAPQKN FASDGGLWLG LFSPAALERA KRIGVSNRWV PDFLNLNTAI
DNSLLNQTYN TPALSTLVTL NNQVQWLNHN GGIDFASART ADSAGRVYSW AEESAVASPY
VVRAEDRSNV ICTIDFDDSV DAAAVAKVLR ANGIVDTEPY RKLGRNQLRI ATFVAIEPDD
ITALTKCIDY VIENI
//
