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Database: UniProt
Entry: Q11RM2_CYTH3
LinkDB: Q11RM2_CYTH3
Original site: Q11RM2_CYTH3 
ID   Q11RM2_CYTH3            Unreviewed;       222 AA.
AC   Q11RM2;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-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};
GN   Name=plsC {ECO:0000313|EMBL:ABG59942.1};
GN   OrderedLocusNames=CHU_2690 {ECO:0000313|EMBL:ABG59942.1};
OS   Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Cytophaga.
OX   NCBI_TaxID=269798 {ECO:0000313|EMBL:ABG59942.1, ECO:0000313|Proteomes:UP000001822};
RN   [1] {ECO:0000313|EMBL:ABG59942.1, ECO:0000313|Proteomes:UP000001822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33406 / NCIMB 9469 {ECO:0000313|Proteomes:UP000001822};
RX   PubMed=17400776; DOI=10.1128/AEM.00225-07;
RA   Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C.,
RA   Gilna P., Han C.S., Lucas S., Misra M., Myers G.L., Richardson P.,
RA   Tapia R., Thayer N., Thompson L.S., Brettin T.S., Henrissat B.,
RA   Wilson D.B., McBride M.J.;
RT   "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT   hutchinsonii.";
RL   Appl. Environ. Microbiol. 73:3536-3546(2007).
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; CP000383; ABG59942.1; -; Genomic_DNA.
DR   STRING; 269798.CHU_2690; -.
DR   EnsemblBacteria; ABG59942; ABG59942; CHU_2690.
DR   KEGG; chu:CHU_2690; -.
DR   eggNOG; ENOG4108F0Q; Bacteria.
DR   eggNOG; COG0204; LUCA.
DR   HOGENOM; HOG000026379; -.
DR   KO; K00655; -.
DR   OMA; RIKLWVF; -.
DR   OrthoDB; 1756450at2; -.
DR   BioCyc; CHUT269798:G1G6N-2648-MONOMER; -.
DR   Proteomes; UP000001822; 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:ABG59942.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001822};
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:UP000001822};
KW   Transferase {ECO:0000256|RuleBase:RU361267,
KW   ECO:0000313|EMBL:ABG59942.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     68     85       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     91    109       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       60    174       PlsC. {ECO:0000259|SMART:SM00563}.
SQ   SEQUENCE   222 AA;  24388 MW;  C8B51C9A187E8DB7 CRC64;
     MIIWSILCIT SSIVVRILTF STHLGVAMAR TVWAPVILWM AGIKLTVKGL EHIPAEKKPY
     IVVSNHQSVI DIPILFYVLP FNVYFVAKKE IAKVPFIGWY MYMMGMIFID RGSRDKALQS
     MINAGTLIRE GKSVMTFPEG TRSLNEKIGV FKAGTFVMAE KAGVEILPVK ISGAGKIWPS
     GGFTIKRGPV TVSIGAPIST AGLNDQTRAK FIEEVKGRVE GL
//
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