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Database: UniProt
Entry: R6WR61_9FIRM
LinkDB: R6WR61_9FIRM
Original site: R6WR61_9FIRM 
ID   R6WR61_9FIRM            Unreviewed;       238 AA.
AC   R6WR61;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   05-DEC-2018, entry version 14.
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=BN605_00124 {ECO:0000313|EMBL:CDD06441.1};
OS   Dorea sp. CAG:317.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Dorea; environmental samples.
OX   NCBI_TaxID=1262873 {ECO:0000313|EMBL:CDD06441.1, ECO:0000313|Proteomes:UP000018262};
RN   [1] {ECO:0000313|EMBL:CDD06441.1, ECO:0000313|Proteomes:UP000018262}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:317 {ECO:0000313|Proteomes:UP000018262};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-2012) 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:CDD06441.1}.
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DR   EMBL; CBGJ010000002; CDD06441.1; -; Genomic_DNA.
DR   Proteomes; UP000018262; 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   Complete proteome {ECO:0000313|Proteomes:UP000018262};
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:UP000018262};
KW   Transferase {ECO:0000256|RuleBase:RU361267}.
FT   DOMAIN       70    185       PlsC. {ECO:0000259|SMART:SM00563}.
SQ   SEQUENCE   238 AA;  27595 MW;  386A912990CF6C17 CRC64;
     MKRILMMVFR NILLVPYMWI KLCYHASHVD KYTEEEHYKM LRYITYRANK GGNVIIDVHG
     QENIPKENGF MFFPNHQGMY DVLAIIDACP KPFSVVAKKE VANVPFLKQV FACMKAYMLD
     REDVRQAMEV IVNVTKEVKK GRNYLIFAEG TRSKKGNQIQ DFKGGSFKSA TKARCPIVPV
     ALIDSFKPFD TNSITPVTVQ VHFLEPLLYE EYKDMKTNEI AETVKERIQN KINENIVK
//
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