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Database: UniProt
Entry: C1EDG4_MICCC
LinkDB: C1EDG4_MICCC
Original site: C1EDG4_MICCC 
ID   C1EDG4_MICCC            Unreviewed;       406 AA.
AC   C1EDG4;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=phosphoserine transaminase {ECO:0000256|ARBA:ARBA00013030};
DE            EC=2.6.1.52 {ECO:0000256|ARBA:ARBA00013030};
GN   ORFNames=MICPUN_95387 {ECO:0000313|EMBL:ACO66052.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO66052.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO66052.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA   John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA   Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA   Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA   Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the marine
RT   picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
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; CP001330; ACO66052.1; -; Genomic_DNA.
DR   RefSeq; XP_002504794.1; XM_002504748.1.
DR   AlphaFoldDB; C1EDG4; -.
DR   STRING; 296587.C1EDG4; -.
DR   GeneID; 8247216; -.
DR   KEGG; mis:MICPUN_95387; -.
DR   eggNOG; KOG2790; Eukaryota.
DR   InParanoid; C1EDG4; -.
DR   OMA; WSKRAAG; -.
DR   OrthoDB; 1404347at2759; -.
DR   UniPathway; UPA00135; UER00197.
DR   Proteomes; UP000002009; Chromosome 11.
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   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; IPR022278; Pser_aminoTfrase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43247; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43247:SF1; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR   Pfam; PF00266; Aminotran_5; 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   Reference proteome {ECO:0000313|Proteomes:UP000002009};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576}.
FT   DOMAIN          10..331
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   406 AA;  43658 MW;  54DA006C558D1D4A CRC64;
     MQTPTKWKHN FSAGPSAVDA GVLAKLSAEL ASFEDTGMGL IEHSHRDAGG PVQRCMAATC
     DLVREVLDVP DSHDVLLMHG GAHAMFAGVA MNLGRTMGSK ADFVGDGFWS KRAAGEASKY
     CVVRHVGATS RTLGGVAIPS PSTWNVDPTA AFVHVTANET IDGLEFHVDP TMPPDAPPLV
     GDFTSTLLSR PVDFSKYSVV YASTGKNLGP SGLVVVIARK DLLTGEREMA ITPGVMSWSA
     AAKSAPIQNI WNTPNVFGIR ALQLVLEDCK AKGGVAAMRA RATRRAWSVY DVIDASEGFY
     VNEVEPEFRS TMTIPVKCKT PEIEERFVEE SEKAGFYNLR GHPLFGGLRI TVYNQVPDDA
     VEALVGFMQQ FQMKVTAEEG TMFGANGKTT YANSPPSVLN SFAFMD
//
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