ID A0A097EGP7_9SPHN Unreviewed; 384 AA.
AC A0A097EGP7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-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};
GN ORFNames=MC45_10430 {ECO:0000313|EMBL:AIT06723.1};
OS Sphingomonas taxi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1549858 {ECO:0000313|EMBL:AIT06723.1, ECO:0000313|Proteomes:UP000033200};
RN [1] {ECO:0000313|EMBL:AIT06723.1, ECO:0000313|Proteomes:UP000033200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55669 {ECO:0000313|EMBL:AIT06723.1,
RC ECO:0000313|Proteomes:UP000033200};
RA Zhou Y., Ma T., Liu T.;
RT "Using Illumina technology Improving SMRT sequencing Genome Assembly by
RT RASTools.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CP009571; AIT06723.1; -; Genomic_DNA.
DR RefSeq; WP_038662736.1; NZ_CP009571.1.
DR AlphaFoldDB; A0A097EGP7; -.
DR STRING; 1549858.MC45_10430; -.
DR KEGG; stax:MC45_10430; -.
DR eggNOG; COG1932; Bacteria.
DR HOGENOM; CLU_040283_0_0_5; -.
DR UniPathway; UPA00135; UER00197.
DR Proteomes; UP000033200; 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 CDD; cd01494; AAT_I; 1.
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; 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 NCBIfam; TIGR01365; serC_2; 1.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 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:AIT06723.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000033200};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW Transferase {ECO:0000313|EMBL:AIT06723.1}.
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 384 AA; 41196 MW; 5118896894D37E25 CRC64;
MTDSVTAPDV RGASKPATKP ARPFFSSGPC AKPPGWDASQ LATDSLGRSH RSKIGKQRLQ
YAIDLMRETL GLPDTHRIGI VPGSDTGAFE MAMWTMLGAR PVTTLAWESF GEGWVTDAVK
QLKIDPTVIR ADYGQLPDLN AVDWSNDVLF TWNGTTSGVR VPNADWIPET REGLSFADAT
SGVFAYDIDW AKIDVATFSW QKVLGGEGGH GVLILGPRAV ERLESYTPAW PLPKVFRLVS
KGKLTEGVFK GETINTPSML AVEDVIVSLE WAKSLGESGL IGRSDANAAA LDKIVAERDW
LGHLAADPAT RSKTSVCLTV EGADEAFIKA MASALEKEGA AYDVAGYRDA PPGLRIWCGA
TVDTADIEAL GPWLDWAYAT AKAA
//
