ID A0A0F0KJE5_9MICO Unreviewed; 370 AA.
AC A0A0F0KJE5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 Name=serC {ECO:0000313|EMBL:KJL21022.1};
GN ORFNames=RN50_01989 {ECO:0000313|EMBL:KJL21022.1};
OS Microbacterium foliorum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=104336 {ECO:0000313|EMBL:KJL21022.1, ECO:0000313|Proteomes:UP000033572};
RN [1] {ECO:0000313|EMBL:KJL21022.1, ECO:0000313|Proteomes:UP000033572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12966 {ECO:0000313|EMBL:KJL21022.1,
RC ECO:0000313|Proteomes:UP000033572};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL21022.1}.
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DR EMBL; JYIU01000042; KJL21022.1; -; Genomic_DNA.
DR RefSeq; WP_045254342.1; NZ_JYIU01000042.1.
DR AlphaFoldDB; A0A0F0KJE5; -.
DR KEGG; mfol:DXT68_12280; -.
DR PATRIC; fig|104336.4.peg.2027; -.
DR UniPathway; UPA00135; UER00197.
DR Proteomes; UP000033572; 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:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 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:KJL21022.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000033572};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW Transferase {ECO:0000313|EMBL:KJL21022.1}.
FT DOMAIN 40..327
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 370 AA; 39167 MW; F91A27E6EE83DD51 CRC64;
MAIEIPRDLL PADGRFGCGP SKVRTEQLEA LLAAGPTLLG TSHRQAPVKN LVGSVREHLA
ALFALPDGYE IIVGNGGSTA FWDAAAFGLI EHRSQNLVFG EFGGKFAAAA AAPWLAAPDV
RKAEPGSRTA AEIVDGVDVY AWPHNETSTG VAAPIDRVVA DGALTVIDAT SAAGGIDFDL
TQADVYYFAP QKNLGSDGGL WFAAVSPAAI ERIERIAASD RYIPEFLSLK NALDNSRLNQ
TLNTPALTTL HLLDSQLSWI LSNGGLAWAG ARTAESSGIL YDWAASSAVA TPFVAEAAHR
SPVVVTIDFD DSVDAAAVAK TLRANGIVDT EPYRKLGRNQ LRVATFVSIE PEDVRQLTRS
LDHVLAQQDA
//
