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Database: UniProt
Entry: I1HUV7_BRADI
LinkDB: I1HUV7_BRADI
Original site: I1HUV7_BRADI 
ID   I1HUV7_BRADI            Unreviewed;       491 AA.
AC   I1HUV7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN   Name=100840298 {ECO:0000313|EnsemblPlants:KQK11365};
GN   ORFNames=BRADI_2g59710v3 {ECO:0000313|EMBL:KQK11365.1};
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368 {ECO:0000313|EnsemblPlants:KQK11365};
RN   [1] {ECO:0000313|EMBL:KQK11365.1, ECO:0000313|EnsemblPlants:KQK11365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK11365.1,
RC   ECO:0000313|EnsemblPlants:KQK11365};
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
RN   [2] {ECO:0000313|EMBL:KQK11365.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK11365.1};
RG   The International Brachypodium Initiative;
RA   Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA   Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA   Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT   "WGS assembly of Brachypodium distachyon.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQK11365}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK11365};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
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}.
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DR   EMBL; CM000881; KQK11365.1; -; Genomic_DNA.
DR   RefSeq; XP_014754612.1; XM_014899126.1.
DR   AlphaFoldDB; I1HUV7; -.
DR   STRING; 15368.I1HUV7; -.
DR   EnsemblPlants; KQK11365; KQK11365; BRADI_2g59710v3.
DR   GeneID; 100840298; -.
DR   Gramene; KQK11365; KQK11365; BRADI_2g59710v3.
DR   KEGG; bdi:100840298; -.
DR   eggNOG; KOG2847; Eukaryota.
DR   HOGENOM; CLU_031593_0_0_1; -.
DR   InParanoid; I1HUV7; -.
DR   OMA; RMRGYMD; -.
DR   OrthoDB; 1387at2759; -.
DR   Proteomes; UP000008810; Chromosome 2.
DR   GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
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.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000008810}.
FT   DOMAIN          146..273
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   COILED          324..351
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   491 AA;  54561 MW;  A88A053C96C44F91 CRC64;
     MAAGGGIPWA ERARAVGVQI RNRFRVAPVD RRWVWGRPDG RAASEAVRQW SDRIRDRLRR
     DRAPDQSSTE AASRPSSSAL RFYRKKVGKV VDGAEDSVII RSLQALAVPL IGNACHVFMH
     GLNSVQIYGA EKLEQALHGR PKGKPLLTVS NHVAAMDDPF VIASLLPPSV MMEAQKLRWT
     LCATDRCFTN PILSTFFRSV KVLPVSRGEG IYQKGMDMAL SKLNNGGWVH IFPEGSRSRD
     GGKTVAPAKR GVGRLVMDAD SLPVVIPFVH TGMQDIMPVG KRIPRTGKRV IVVVGDPIHF
     DDLIVDNGED TQHISRGILY DKATERIGQQ LQQLKVEVDR LAAEQKAELQ SRCIDDTVND
     GYRLWQQVDW EAFGIGNMLS SDREPLKQVQ HELLLAEQST SLPKQAEPEL HLEEQSVSPV
     PGAAISPDVG VPHWFRRHSD PSELMGFAAR GLLKNGRFME EGYRQFPDST ALDDVWWGAQ
     ANNAMPRWST A
//
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