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Database: UniProt
Entry: A0A1Y3TKD4_9FIRM
LinkDB: A0A1Y3TKD4_9FIRM
Original site: A0A1Y3TKD4_9FIRM 
ID   A0A1Y3TKD4_9FIRM        Unreviewed;       236 AA.
AC   A0A1Y3TKD4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   05-DEC-2018, entry version 5.
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=B5G27_07750 {ECO:0000313|EMBL:OUN34619.1};
OS   Lachnoclostridium sp. An76.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae.
OX   NCBI_TaxID=1965654 {ECO:0000313|EMBL:OUN34619.1, ECO:0000313|Proteomes:UP000199802};
RN   [1] {ECO:0000313|EMBL:OUN34619.1, ECO:0000313|Proteomes:UP000199802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|EMBL:OUN34619.1,
RC   ECO:0000313|Proteomes:UP000199802};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T.,
RA   Cizek A., Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-
CC         diacyl-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
CC       and may constitute the binding site for the phosphate moiety of
CC       the 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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OUN34619.1}.
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DR   EMBL; NFHL01000003; OUN34619.1; -; Genomic_DNA.
DR   Proteomes; UP000199802; 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:OUN34619.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199802};
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:UP000199802};
KW   Transferase {ECO:0000256|RuleBase:RU361267,
KW   ECO:0000313|EMBL:OUN34619.1}.
FT   DOMAIN       70    185       PlsC. {ECO:0000259|SMART:SM00563}.
SQ   SEQUENCE   236 AA;  27261 MW;  8D400ADCBA420363 CRC64;
     MKRILMMVLR NLYMVPYGWI RLCYRAAHVD KYTEEDMYAF LRWIDLHANR GGRVHIDVHG
     RENIPDRDGF MFFPNHQGLY DVLAIIEASP RPFSVVAKKE IAKIPFLKQI FACMKAFMLD
     REDVRQAMQV IINVTKEVQK GRNYLIFAEG TRSKNGNRVG SFKGGSFKAA TKARCPIVPV
     ALIDSFKPFD TNTIRPVTVQ VHFLKPLEYE EYKDMKTTEI AALVEKRIQS VIDANI
//
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