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Database: UniProt
Entry: G0VGA6_NAUCC
LinkDB: G0VGA6_NAUCC
Original site: G0VGA6_NAUCC 
ID   G0VGA6_NAUCC            Unreviewed;       395 AA.
AC   G0VGA6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Phosphoserine aminotransferase {ECO:0000256|RuleBase:RU004505};
DE            EC=2.6.1.52 {ECO:0000256|RuleBase:RU004505};
GN   Name=NCAS0F00420 {ECO:0000313|EMBL:CCC70526.1};
GN   OrderedLocusNames=NCAS_0F00420 {ECO:0000313|EMBL:CCC70526.1};
OS   Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS   1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC70526.1, ECO:0000313|Proteomes:UP000001640};
RN   [1] {ECO:0000313|EMBL:CCC70526.1, ECO:0000313|Proteomes:UP000001640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC   {ECO:0000313|Proteomes:UP000001640};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain:CBS 4309;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Genome sequence of Naumovozyma castellii.";
RL   Submitted (AUG-2011) 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; HE576757; CCC70526.1; -; Genomic_DNA.
DR   RefSeq; XP_003676882.1; XM_003676834.1.
DR   AlphaFoldDB; G0VGA6; -.
DR   STRING; 1064592.G0VGA6; -.
DR   GeneID; 11527466; -.
DR   KEGG; ncs:NCAS_0F00420; -.
DR   eggNOG; KOG2790; Eukaryota.
DR   HOGENOM; CLU_034866_0_0_1; -.
DR   InParanoid; G0VGA6; -.
DR   OMA; AFVYFCD; -.
DR   OrthoDB; 1404347at2759; -.
DR   UniPathway; UPA00135; UER00197.
DR   Proteomes; UP000001640; Chromosome 6.
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; 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   PIRSF; PIRSF000525; SerC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
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   Reference proteome {ECO:0000313|Proteomes:UP000001640};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299,
KW   ECO:0000256|RuleBase:RU004505};
KW   Transferase {ECO:0000256|RuleBase:RU004505}.
FT   DOMAIN          11..383
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   395 AA;  43746 MW;  DB55EB3AB3C0E7BF CRC64;
     MSLEREEPTH FGAGPAQLPT EVLQQAAKDL INYNNLGLGI GEISHRSKDA TKVIEDSKLH
     LKELMNIPDT HEVFFMQGGG TTGFSSLATN LAAAYVGKTG TIAPAGYLVT GSWSLKSYQE
     ANRLHVPAEI IFNAKDYHGG KFGYIPKEEE WCDKVKGKKY SFVYLCENET VHGVEWPKLP
     QCLVDDNEIE IVADLSSDIL SRQVDVSQYG VIMAGAQKNI GLAGLTVYII KKSILKNIEK
     ADETQLHEFG IPVTPIASDY PTVVKNNSAY NTIPIFTLHV MDLVFQHLIK KGGVASQEAE
     NKTKAKILYE ALDSYPDFYN MPVEKSCRST MNVVFTLKKE GLDDKFLEEA GKRKLTGLKG
     HRSVGGFRAS IYNALSLATI EKLVKFVKEF AEENQ
//
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