UniProt: N1RT98

Database: UniProt
Entry: N1RT98_FUSC4

LinkDB:  N1RT98_FUSC4 
Original site:  N1RT98_FUSC4

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (3)   
   Pfam (1)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (13)   

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ID   N1RT98_FUSC4            Unreviewed;       488 AA.
AC   N1RT98;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   22-FEB-2023, entry version 29.
DE   RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0000256|RuleBase:RU365024};
DE            EC=2.7.8.5 {ECO:0000256|RuleBase:RU365024};
GN   ORFNames=FOC4_g10008306 {ECO:0000313|EMBL:EMT69868.1};
OS   Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT69868.1, ECO:0000313|Proteomes:UP000016929};
RN   [1] {ECO:0000313|Proteomes:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA   Fang X., Huang J.;
RT   "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT   banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX   PubMed=24743270;
RA   Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA   Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA   Fang X., Peng M., Huang J.;
RT   "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT   oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL   PLoS ONE 9:E95543-E95543(2014).
CC   -!- FUNCTION: Functions in the biosynthesis of the anionic phospholipids
CC       phosphatidylglycerol and cardiolipin. {ECO:0000256|RuleBase:RU365024}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-
CC         diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP +
CC         H(+); Xref=Rhea:RHEA:12593, ChEBI:CHEBI:15378, ChEBI:CHEBI:57597,
CC         ChEBI:CHEBI:58332, ChEBI:CHEBI:60110, ChEBI:CHEBI:60377; EC=2.7.8.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001566,
CC         ECO:0000256|RuleBase:RU365024};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC       phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005042, ECO:0000256|RuleBase:RU365024}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU365024}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-II
CC       family. {ECO:0000256|ARBA:ARBA00010682, ECO:0000256|RuleBase:RU365024}.
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DR   EMBL; KB726324; EMT69868.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1RT98; -.
DR   STRING; 1229665.N1RT98; -.
DR   HOGENOM; CLU_030471_1_1_1; -.
DR   UniPathway; UPA00084; UER00503.
DR   Proteomes; UP000016929; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR   CDD; cd09135; PLDc_PGS1_euk_1; 1.
DR   CDD; cd09137; PLDc_PGS1_euk_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   InterPro; IPR016270; PGS1.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   PANTHER; PTHR12586:SF1; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12586; CDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   PIRSF; PIRSF000850; Phospholipase_D_PSS; 2.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR   PROSITE; PS50035; PLD; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU365024};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU365024};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU365024};
KW   Mitochondrion {ECO:0000256|RuleBase:RU365024};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU365024};
KW   Phospholipid biosynthesis {ECO:0000256|RuleBase:RU365024};
KW   Phospholipid metabolism {ECO:0000256|RuleBase:RU365024};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016929};
KW   Transferase {ECO:0000256|RuleBase:RU365024, ECO:0000313|EMBL:EMT69868.1}.
FT   DOMAIN          150..176
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   488 AA;  54563 MW;  702C235EB6AD8372 CRC64;
     MPAGNTPPSV NSVGALAPFV TELDRLAPSF DVRGEQIQII RTPAEFYETL KDRIRKAQRR
     IFLSTLYIGK SEKELIETLQ EALRKNPDVK LSILTDALRG TREAPNPSSA SLLAPLVEEF
     GADRVEIRMY HTPNLTGLRK QYIPKRINEG WGLQHMKLYG VDDEIIMSGA NLSTDYFTNR
     QDRYHLFASK EVTDHFWKIH SGVTSFSFLV QPSTEPAGFT LSWPENNSAP SPLEKPQSFI
     KSTTSTLQTL LHPTSKPEND ISDTRVYMLG QMSQVMKPDT STELPVITHI LKTLALPAYR
     ESSWTFTAGY FNPAPSLTKL LLNTASTSNT VITASPEANG FYKSKGVSGL LPDAYTLLAR
     RFVHRVHHEG RDNDITLKEW RYGVVGQPGG WTYHAKGLWV TMPGDKNPAM SIIGSSNYTK
     RSYSHDLEAG ALIVTRDEGL KGRLGEEQLW LQEHATKATR DDFARTERRV GLKVRVAMWI
     VSLVGGAL
//

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