ID W0AN19_9SPHN Unreviewed; 375 AA.
AC W0AN19;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=phosphoserine transaminase {ECO:0000256|ARBA:ARBA00013030};
DE EC=2.6.1.52 {ECO:0000256|ARBA:ARBA00013030};
GN ORFNames=NX02_27525 {ECO:0000313|EMBL:AHE57090.1};
OS Sphingomonas sanxanigenens DSM 19645 = NX02.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1123269 {ECO:0000313|EMBL:AHE57090.1, ECO:0000313|Proteomes:UP000018851};
RN [1] {ECO:0000313|EMBL:AHE57090.1, ECO:0000313|Proteomes:UP000018851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NX02 {ECO:0000313|EMBL:AHE57090.1,
RC ECO:0000313|Proteomes:UP000018851};
RA Ma T., Huang H., Wu M., Li X., Li G.;
RT "Completed genome of Sphingomonas sanxanigenens NX02.";
RL Submitted (JUL-2013) 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; CP006644; AHE57090.1; -; Genomic_DNA.
DR RefSeq; WP_025295187.1; NZ_CP006644.1.
DR AlphaFoldDB; W0AN19; -.
DR STRING; 1123269.NX02_27525; -.
DR KEGG; ssan:NX02_27525; -.
DR PATRIC; fig|1123269.5.peg.5401; -.
DR eggNOG; COG1932; Bacteria.
DR HOGENOM; CLU_040283_0_0_5; -.
DR OrthoDB; 9772439at2; -.
DR UniPathway; UPA00135; UER00197.
DR Proteomes; UP000018851; 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:AHE57090.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000018851};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW Transferase {ECO:0000313|EMBL:AHE57090.1}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 375 AA; 40304 MW; C9264C1DE012C156 CRC64;
MTTITRPGTK PARPYFSSGP CAKPPGWSAE KLNPESLGRS HRSKIGKARL KYCIDLMREL
LRLPDTHRIG IVPGSDTGAF EMAMWTMLGA RPVTTLAWES FGEGWVTDAV KQLKLDPTIL
RADYGQLPDL TQVDWSNDVL FTWNGTTSGV RVPNGDWIAD DRAGLAFADA TSAVFAYDLP
WDKIDVATFS WQKVLGGEGG HGVLILGPRA VERLETHTPA WPLPKVFRLV SKGALAEGVF
KGETINTPSM LAVEDAISAL EWAKSVGGAD GLIARSDANA AALDKIVEDR AWLGHLAADP
ASRSTTSVCL TVAGADEALI KKIASLLEAE DAAYDVAGYR DAPAGLRIWC GATVDTADIE
ALGPWLDWAY ETAKA
//
