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Database: UniProt
Entry: H2AXA5_KAZAF
LinkDB: H2AXA5_KAZAF
Original site: H2AXA5_KAZAF 
ID   H2AXA5_KAZAF            Unreviewed;       252 AA.
AC   H2AXA5;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=CDP-diacylglycerol--serine O-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00017171, ECO:0000256|PIRNR:PIRNR000852};
DE            EC=2.7.8.8 {ECO:0000256|ARBA:ARBA00013174, ECO:0000256|PIRNR:PIRNR000852};
DE   AltName: Full=Phosphatidylserine synthase {ECO:0000256|ARBA:ARBA00032361, ECO:0000256|PIRNR:PIRNR000852};
GN   Name=KAFR0F04100 {ECO:0000313|EMBL:CCF59005.1};
GN   ORFNames=KAFR_0F04100 {ECO:0000313|EMBL:CCF59005.1};
OS   Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS   1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF59005.1, ECO:0000313|Proteomes:UP000005220};
RN   [1] {ECO:0000313|EMBL:CCF59005.1, ECO:0000313|Proteomes:UP000005220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC   NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-
CC         glycero-3-phospho-L-serine + CMP + H(+); Xref=Rhea:RHEA:16913,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262,
CC         ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00000287,
CC         ECO:0000256|PIRNR:PIRNR000852};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC       1/2. {ECO:0000256|PIRNR:PIRNR000852}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC       family. {ECO:0000256|PIRNR:PIRNR000852, ECO:0000256|RuleBase:RU003750}.
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DR   EMBL; HE650826; CCF59005.1; -; Genomic_DNA.
DR   RefSeq; XP_003958140.1; XM_003958091.1.
DR   AlphaFoldDB; H2AXA5; -.
DR   STRING; 1071382.H2AXA5; -.
DR   GeneID; 13884530; -.
DR   KEGG; kaf:KAFR_0F04100; -.
DR   eggNOG; ENOG502QPJG; Eukaryota.
DR   HOGENOM; CLU_049944_5_0_1; -.
DR   InParanoid; H2AXA5; -.
DR   OrthoDB; 1332156at2759; -.
DR   UniPathway; UPA00558; UER00615.
DR   Proteomes; UP000005220; Chromosome 6.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003882; F:CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006659; P:phosphatidylserine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   InterPro; IPR004533; CDP-diaglyc--ser_O-PTrfase.
DR   InterPro; IPR016271; CDP-diaglyc--ser_O-PTrfase_fun.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR   NCBIfam; TIGR00473; pssA; 1.
DR   PANTHER; PTHR14269; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR14269:SF61; CDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE; 1.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   PIRSF; PIRSF000852; Phosphatidylserine_synth_fun; 1.
DR   PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR000852};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|PIRNR:PIRNR000852};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|PIRNR:PIRNR000852};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000852};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW   ECO:0000256|PIRNR:PIRNR000852};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264,
KW   ECO:0000256|PIRNR:PIRNR000852};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000852};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        73..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   252 AA;  28675 MW;  476D09CE70007476 CRC64;
     MESELRQRSV TEDHESDIDQ LSIASEHHLS KKSSTIFTID TTPLAPPNEN DIDLFTSDKY
     HFSMIRNLHM ADFITMLNGF SGFYSIVSCL RFTLTKKSYY VQRAHLFIFL GTVFDFLDGR
     VARLRNRSSL MGQELDSLAD LISFGVAPAS IAFAIGFQTT LDVFILSFFV LCGLCRLARF
     NVTVGQLPKD KKGKSKFFEG FPMPTTLFEV CGMELLIKLN RFNDEVPFGI IRKGKFLEFH
     PLVLIFSFMD VV
//
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