GenomeNet

Database: UniProt
Entry: A0A0U1L3T8_9FIRM
LinkDB: A0A0U1L3T8_9FIRM
Original site: A0A0U1L3T8_9FIRM 
ID   A0A0U1L3T8_9FIRM        Unreviewed;       202 AA.
AC   A0A0U1L3T8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   11-DEC-2019, entry version 11.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|RuleBase:RU361267};
DE            EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267};
GN   ORFNames=SpAn4DRAFT_0798 {ECO:0000313|EMBL:CQR74336.1};
OS   Sporomusa sp. An4.
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Sporomusa; unclassified Sporomusa.
OX   NCBI_TaxID=411922 {ECO:0000313|EMBL:CQR74336.1, ECO:0000313|Proteomes:UP000049855};
RN   [1] {ECO:0000313|EMBL:CQR74336.1, ECO:0000313|Proteomes:UP000049855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sporomusa ovata strain An4 {ECO:0000313|EMBL:CQR74336.1};
RA   Murphy D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC         ChEBI:CHEBI:58608; EC=2.3.1.51;
CC         Evidence={ECO:0000256|RuleBase:RU361267};
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC       may constitute the binding site for the phosphate moiety of the
CC       glycerol-3-phosphate. {ECO:0000256|RuleBase:RU361267}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|RuleBase:RU361267}.
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; CTRP01000014; CQR74336.1; -; Genomic_DNA.
DR   RefSeq; WP_021170338.1; NZ_CTRP01000014.1.
DR   EnsemblBacteria; CQR74336; CQR74336; SpAn4DRAFT_0798.
DR   Proteomes; UP000049855; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR004552; AGP_acyltrans.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   TIGRFAMs; TIGR00530; AGP_acyltrn; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361267,
KW   ECO:0000313|EMBL:CQR74336.1};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000049855};
KW   Transferase {ECO:0000256|RuleBase:RU361267, ECO:0000313|EMBL:CQR74336.1}.
FT   DOMAIN          32..144
FT                   /note="PlsC"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   202 AA;  21911 MW;  B2572092E9B50671 CRC64;
     MYELLRMFFA VLFSIAFRWR TFGIENIPAG GAIIAANHIS LWDPPVVGTA LPRRAHFMAK
     EELFANPVFG WLISKLGAFP VKRGAADRTA IKTALTLLKK GSILVIFPEG TRSKDGKLGT
     PEAGLALLAL KAGVPVIPAA ITGTNKIFRA GHVLPKFCIR FGKPILPGCD NAGKESMEKM
     STQVMTEISY LLEEADSITK QV
//
DBGET integrated database retrieval system