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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//