ID A0A0H5C4G8_CYBJN Unreviewed; 380 AA.
AC A0A0H5C4G8; A0A1E4RWQ0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Tafazzin family protein {ECO:0000256|RuleBase:RU365062};
GN Name=TAZ1 {ECO:0000313|EMBL:CEP22863.1};
GN ORFNames=BN1211_3321 {ECO:0000313|EMBL:CEP22863.1}, CYBJADRAFT_131152
GN {ECO:0000313|EMBL:ODV71650.1};
OS Cyberlindnera jadinii (strain ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617
OS / NBRC 0987 / NRRL Y-1542) (Torula yeast) (Candida utilis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=983966 {ECO:0000313|EMBL:CEP22863.1, ECO:0000313|Proteomes:UP000038830};
RN [1] {ECO:0000313|EMBL:CEP22863.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS1600 {ECO:0000313|EMBL:CEP22863.1};
RA Jaenicke S.;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000038830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 /
RC NRRL Y-1542 {ECO:0000313|Proteomes:UP000038830};
RX PubMed=26150016; DOI=10.1016/j.jbiotec.2015.06.423;
RA Rupp O., Brinkrolf K., Buerth C., Kunigo M., Schneider J., Jaenicke S.,
RA Goesmann A., Puehler A., Jaeger K.-E., Ernst J.F.;
RT "The structure of the Cyberlindnera jadinii genome and its relation to
RT Candida utilis analyzed by the occurrence of single nucleotide
RT polymorphisms.";
RL J. Biotechnol. 211:20-30(2015).
RN [3] {ECO:0000313|EMBL:ODV71650.1, ECO:0000313|Proteomes:UP000094389}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 /
RC NRRL Y-1542 {ECO:0000313|Proteomes:UP000094389}, and NRRL Y-1542
RC {ECO:0000313|EMBL:ODV71650.1};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-
CC phospho]-glycerol + a 1,2-diacyl-sn-glycero-3-phosphocholine = a 1-
CC acyl-sn-glycero-3-phosphocholine + a cardiolipin;
CC Xref=Rhea:RHEA:33731, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:62237, ChEBI:CHEBI:64743;
CC Evidence={ECO:0000256|ARBA:ARBA00024570};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33732;
CC Evidence={ECO:0000256|ARBA:ARBA00024570};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:33733;
CC Evidence={ECO:0000256|ARBA:ARBA00024570};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004137}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004137}; Intermembrane side
CC {ECO:0000256|ARBA:ARBA00004137}. Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00024323}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00024323}; Intermembrane side
CC {ECO:0000256|ARBA:ARBA00024323}.
CC -!- SIMILARITY: Belongs to the taffazin family.
CC {ECO:0000256|ARBA:ARBA00010524, ECO:0000256|RuleBase:RU365062}.
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DR EMBL; CDQK01000003; CEP22863.1; -; Genomic_DNA.
DR EMBL; KV453939; ODV71650.1; -; Genomic_DNA.
DR RefSeq; XP_020068689.1; XM_020212962.1.
DR STRING; 983966.A0A0H5C4G8; -.
DR GeneID; 30987358; -.
DR OMA; IMRYFKW; -.
DR OrthoDB; 1387at2759; -.
DR Proteomes; UP000038830; Unassembled WGS sequence.
DR Proteomes; UP000094389; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR InterPro; IPR000872; Tafazzin.
DR PANTHER; PTHR12497:SF0; TAFAZZIN; 1.
DR PANTHER; PTHR12497; TAZ PROTEIN TAFAZZIN; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR PRINTS; PR00979; TAFAZZIN.
DR SMART; SM00563; PlsC; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Reference proteome {ECO:0000313|Proteomes:UP000094389}.
FT DOMAIN 71..241
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 380 AA; 44010 MW; 09BE29ED8D2C6415 CRC64;
MSLPQVLERG DDVLSDLPRR SVWWNWASQA TCMAVVGFSK TVLNLFYEPH LHGLENLDRA
LSKAREENRG LVTVMNHMSV VDDPFMWGFL PWRFFTDLDD IRWGLAASNL CFANKASSYF
FSLGKIFGTE RLGGSPFQGC IDAAIRVMSP DDTLDLIYDG SSTTDKVWLN EKEVFHKVKQ
NYLSPMIRSK PSWLHVFPEG FVLQLQAPFA NSMRYFHWGI TRIILESTRQ PVIVPMFAHG
FEKIAPEAED EGVMNRFLPS NIGAEVHMYI SKAIDDEVIH KYREEWLALV KKYGDGKDLT
QELRFGEKAQ ELRSRLANEL RQQVARIRRE IGFPEEDTRF SDPKWWRQFT KTEGKSDPEV
RFNGLNWAIR RLHGLPEKDD
//
