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Database: UniProt
Entry: Q07XC2_SHEFN
LinkDB: Q07XC2_SHEFN
Original site: Q07XC2_SHEFN 
ID   Q07XC2_SHEFN            Unreviewed;       244 AA.
AC   Q07XC2;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   13-NOV-2019, entry version 69.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|RuleBase:RU361267};
DE            EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267};
DE   Flags: Precursor;
GN   OrderedLocusNames=Sfri_3514 {ECO:0000313|EMBL:ABI73342.1};
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI73342.1, ECO:0000313|Proteomes:UP000000684};
RN   [1] {ECO:0000313|EMBL:ABI73342.1, ECO:0000313|Proteomes:UP000000684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI73342.1,
RC   ECO:0000313|Proteomes:UP000000684};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T.,
RA   Nealson K.H., Newman D., Tiedje J.M., Zhou J., Romine M.F.,
RA   Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) 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}.
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DR   EMBL; CP000447; ABI73342.1; -; Genomic_DNA.
DR   RefSeq; WP_011638933.1; NC_008345.1.
DR   STRING; 318167.Sfri_3514; -.
DR   EnsemblBacteria; ABI73342; ABI73342; Sfri_3514.
DR   KEGG; sfr:Sfri_3514; -.
DR   eggNOG; ENOG4107S7E; Bacteria.
DR   eggNOG; COG0204; LUCA.
DR   HOGENOM; HOG000026378; -.
DR   KO; K00655; -.
DR   OMA; RIKLWVF; -.
DR   OrthoDB; 1756450at2; -.
DR   BioCyc; SFRI318167:G1G77-3644-MONOMER; -.
DR   Proteomes; UP000000684; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:ABI73342.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000684};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000684};
KW   Transferase {ECO:0000256|RuleBase:RU361267,
KW   ECO:0000313|EMBL:ABI73342.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     35     54       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       67    182       PlsC. {ECO:0000259|SMART:SM00563}.
FT   COILED      221    241       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   244 AA;  27094 MW;  74992C9827445BC9 CRC64;
     MLLIARSIIL AVLLFLLFVF SIVFCLLRPM HRNNVHVIAS IFGSVAPILG IKVIKRVHPV
     SATSEPCIYL ANHQNNFDLF THTSVVPKAT VSLGKKSLAW MPLFGQIYWL SGNILIDRKN
     RHSAFDTMAK TVERMKNKGL SVWIFPEGTR SRGRGLLPFK VGAFHTAIAA QAPIVPVLAS
     CQSHINLNRW NNGVVIVEMM EPIPTAGLDK NDVKALNTKV HQLMSARLVE LNKEAEALTL
     KART
//
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