ID Q1NEW3_SPHSS Unreviewed; 396 AA.
AC Q1NEW3;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=phosphoserine transaminase {ECO:0000256|ARBA:ARBA00013030};
DE EC=2.6.1.52 {ECO:0000256|ARBA:ARBA00013030};
GN ORFNames=SKA58_15667 {ECO:0000313|EMBL:EAT09748.1};
OS Sphingomonas sp. (strain SKA58).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=314266 {ECO:0000313|EMBL:EAT09748.1, ECO:0000313|Proteomes:UP000005395};
RN [1] {ECO:0000313|EMBL:EAT09748.1, ECO:0000313|Proteomes:UP000005395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA58 {ECO:0000313|EMBL:EAT09748.1,
RC ECO:0000313|Proteomes:UP000005395};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (MAR-2006) 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}.
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:EAT09748.1}.
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DR EMBL; AAQG01000003; EAT09748.1; -; Genomic_DNA.
DR RefSeq; WP_009822881.1; NZ_CH959307.1.
DR AlphaFoldDB; Q1NEW3; -.
DR STRING; 314266.SKA58_15667; -.
DR eggNOG; COG1932; Bacteria.
DR HOGENOM; CLU_040283_0_0_5; -.
DR OrthoDB; 9772439at2; -.
DR UniPathway; UPA00135; UER00197.
DR Proteomes; UP000005395; 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 ECO:0000313|EMBL:EAT09748.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000005395};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW Transferase {ECO:0000313|EMBL:EAT09748.1}.
SQ SEQUENCE 396 AA; 42997 MW; 0D93FC9C98CEA9F5 CRC64;
MTDLTAADAT IAPAAKPATT PARPFFSSGP CAKPPVWSAD KLSTDSLGRS HRAKIGKSRL
AYCIDLMREI LQLPDTHRIG IVPGSDTGAF EMAMWTMLGA RPVTTLAWES FGEGWVTDAA
KQLKLDPTII RADYGQLPDL AQVDFSHDVL FTWNGTTSGV RVPNADWIPS TREGLTFADA
TSAVFAYDID WTKIDVATFS WQKVLGGEGG HGVLILGPRA VERLETHTPA WPLPKVFRLM
AKGKLAEGIF KGETINTPSM LAVEDAIFAL EWGKSLGGLD GLIARSDANA AALDKIVADR
DWLHHLAAEP EYRSKTSVCL YVALFDQDMI KRFASLLEKE GAAYDIAGYR DAPAGLRIWC
GATVDTADID ALGPWLDWAY ATVKAEEQAK HEAPHS
//
