ID V4NFR5_9CAUL Unreviewed; 424 AA.
AC V4NFR5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=phosphoserine transaminase {ECO:0000256|ARBA:ARBA00013030};
DE EC=2.6.1.52 {ECO:0000256|ARBA:ARBA00013030};
GN ORFNames=ABENE_22325 {ECO:0000313|EMBL:ESQ80702.1};
OS Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1121022 {ECO:0000313|EMBL:ESQ80702.1, ECO:0000313|Proteomes:UP000017837};
RN [1] {ECO:0000313|EMBL:ESQ80702.1, ECO:0000313|Proteomes:UP000017837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16100 {ECO:0000313|EMBL:ESQ80702.1,
RC ECO:0000313|Proteomes:UP000017837};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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:ESQ80702.1}.
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DR EMBL; AWGB01000095; ESQ80702.1; -; Genomic_DNA.
DR AlphaFoldDB; V4NFR5; -.
DR STRING; 1121022.GCA_000376105_04342; -.
DR PATRIC; fig|1121022.4.peg.4571; -.
DR eggNOG; COG1932; Bacteria.
DR UniPathway; UPA00135; UER00197.
DR Proteomes; UP000017837; 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 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000017837};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW Transferase {ECO:0000256|ARBA:ARBA00022576}.
FT REGION 29..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 46292 MW; 764E81FFB3B56889 CRC64;
MYASCMYFML IVYASPIITL AMQNPMNRAM PPRPATKPGN PNFSSGPCAK RPGWRASDLD
SAILGRSHRS PIAKTRINAV VSLTREVLGI PQDYRIGIVP GSDTGAMEMA LWNLLGSRGV
DVLAWDVFGA EWVRDAAMEL QLTDLRVFQA PYGQLPDLSQ TSADRDIVFT WNGTSTGVRV
PNADWISDAR TGLTICDATS AAFAMALPWE KLDVTTWSWQ KVLGGEGAHG VIVLSPRAIK
RLTTYRPPRP IPKIFRLTDG NTVKEGIFTG DTINTPSMLV IEDALDGLAW AKSIGGVPAL
VRHGEANLDL LSNWIEKSKW ASFLAEAPDT RSTTSLCVKV GEADVLRWPR MQQEALIRGV
TEYLETEGAA YDIAAYRGVT IGFRLWAGAT VATADLSVAL DWLDYAYFIV KSRLAPGPTS
QVSK
//
