ID B8LRT6_PICSI Unreviewed; 433 AA.
AC B8LRT6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Phosphoserine aminotransferase {ECO:0000256|RuleBase:RU004505};
DE EC=2.6.1.52 {ECO:0000256|RuleBase:RU004505};
OS Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3332 {ECO:0000313|EMBL:ABR18366.1};
RN [1] {ECO:0000313|EMBL:ABR18366.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Bark {ECO:0000313|EMBL:ABR18366.1};
RA Ralph S.G., Chun H.E., Liao N., Ali J., Reid K., Kolosova N., Cooper N.,
RA Cullis C., Jancsik S., Moore R., Mayo M., Wagner S., Holt R.A.,
RA Jones S.J.M., Marra M.A., Ritland C.E., Ritland K., Bohlmann J.;
RT "Full length cDNA sequences from Sitka Spruce (Picea sitchensis).";
RL Submitted (JUN-2007) 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 ECO:0000256|RuleBase:RU004505};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004504};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 2/3. {ECO:0000256|ARBA:ARBA00005099,
CC ECO:0000256|RuleBase:RU004505}.
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; EF678631; ABR18366.1; -; mRNA.
DR AlphaFoldDB; B8LRT6; -.
DR OMA; AFVYFCD; -.
DR UniPathway; UPA00135; UER00197.
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; cd00611; PSAT_like; 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 HAMAP; MF_00160; SerC_aminotrans_5; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR022278; Pser_aminoTfrase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01364; serC_1; 1.
DR PANTHER; PTHR43247; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43247:SF1; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU004505};
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000256|RuleBase:RU004505};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299,
KW ECO:0000256|RuleBase:RU004505};
KW Transferase {ECO:0000256|RuleBase:RU004505}.
FT DOMAIN 75..422
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 433 AA; 47426 MW; AF96C8693E660EFC CRC64;
MATSATFQQT FLLNNNLGSL SSITGTKLCT PSLCLREKTH DSSRKTLSVT CTAVVPSSAT
PRTGFSDPVQ EEGRVFNFAA GPATLPENVI KKAQAELYNW RGSGMSIMEV SHRGKEFTSV
IQKAESDLRE LLSIPANYEV LFLQGGASTQ FSCLPLNLCG VEDTADYIVT GSWGDKAFKE
GQRFCKANLA WSGKATKYTR VPAEEEIQLN PNAKYLHICA NETIHGVEFK DYPTPKGDTT
FLVADMSSNF CSKPVDVSKF GLIYAGAQKN VGPAGVTIVI IRNDLIGHAQ QSTPLMLDYK
IHAENKSLYN TPPCFTIYMC GLVFEDLLAQ GGLNEIEKKN VQKAKILYDA IDASNGFYRC
PVEKSVRSLM NVPFTLEKSE LESDFIKQAA SEGMLQLKGH RSVGGMRASI YNAMPLAGVE
KLVSFMKVFQ ANH
//