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Database: UniProt/TrEMBL
Entry: D3RTC5_ALLVD
LinkDB: D3RTC5_ALLVD
Original site: D3RTC5_ALLVD 
ID   D3RTC5_ALLVD            Unreviewed;       947 AA.
AC   D3RTC5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   30-AUG-2017, entry version 43.
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   OrderedLocusNames=Alvin_1501 {ECO:0000313|EMBL:ADC62434.1};
OS   Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 /
OS   NCIMB 10441 / D) (Chromatium vinosum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Chromatiaceae; Allochromatium.
OX   NCBI_TaxID=572477 {ECO:0000313|EMBL:ADC62434.1, ECO:0000313|Proteomes:UP000001441};
RN   [1] {ECO:0000313|EMBL:ADC62434.1, ECO:0000313|Proteomes:UP000001441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D
RC   {ECO:0000313|Proteomes:UP000001441};
RX   PubMed=22675582; DOI=10.4056/sigs.2335270;
RA   Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA   Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT   "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL   Stand. Genomic Sci. 5:311-330(2011).
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate =
CC       CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
CC       {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; CP001896; ADC62434.1; -; Genomic_DNA.
DR   RefSeq; WP_012970708.1; NC_013851.1.
DR   ProteinModelPortal; D3RTC5; -.
DR   STRING; 572477.Alvin_1501; -.
DR   EnsemblBacteria; ADC62434; ADC62434; Alvin_1501.
DR   KEGG; alv:Alvin_1501; -.
DR   eggNOG; ENOG4107RCI; Bacteria.
DR   eggNOG; COG0318; LUCA.
DR   HOGENOM; HOG000026854; -.
DR   OMA; VPVDFMS; -.
DR   OrthoDB; POG091H0HAF; -.
DR   Proteomes; UP000001441; 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; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   TIGRFAMs; TIGR00530; AGP_acyltrn; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361267,
KW   ECO:0000313|EMBL:ADC62434.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001441};
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:UP000001441};
KW   Transferase {ECO:0000256|RuleBase:RU361267,
KW   ECO:0000313|EMBL:ADC62434.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    347    370       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    718    736       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       27    102       Carrier. {ECO:0000259|PROSITE:PS50075}.
FT   MOD_RES      67     67       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00258}.
SQ   SEQUENCE   947 AA;  103539 MW;  E8BCAB585E992A60 CRC64;
     MTSHPHPTDE RHEAAPAHST TPVHDEPARR LLSVLSDFVR ESHLPEPREG LTLDTRLESD
     LGLDSLSRSE LIARIERGLN IQLPDTALLA DTPRELLARM RGTPDTQAGG SQGVTLAAPT
     GAGLEHPSGA RTLLDVLAWH RDRQGERVHL TYYDGDDRPH PLTHAALAEG AERVAARLHA
     AGLKSGGTVA IMLPTGLDYF FAFFGVLIAG GVPVPIYPPA RPQQLEDHLR RHARLLDNAG
     VCVLITVSEA RHVARLLSAQ VPSLHEILTL ETPDETAPLS RADWAAPNAG DLAFLQYTSG
     STGDPKGVML THADLLANIR AMGEAIAIAP DDVFVSWLPL YHDMGLIGAW LGSLYFGVPL
     IVMSPLAFLA RPRRWLQAIS AHRGTLSAAP NFAYELCLTR LSDSQLEGLD LRSWRRAFNG
     AEPVSAETLH RFAERFAPCG LRPEALAPVY GLAEAAVGLA FPPVERGPRI DCIDRARFAG
     SGYALPVACD DPDAMAVVAC GRPLPGYRVR VVDESGRERP ERHEGLLQFQ GPSATQGYYR
     HPEATARLIR DGWHETGDRA YLAGGDIHLT GRVKDLIIRG GRNLYPYEVE QALGELTGIR
     RGCVVAFAAR DARQGSERLV IVAESKERDP ERRAALAQRA RERATEVLGL PPDEIVLAPP
     RAVLKTSSGK LRRGDTRERY LAGRLFDTPP APVWQLARVG ARAVLARLRT WGVRLPETLY
     AGYAWGVFTL LAPWVWGGVM LSPRPAWRWS LARGGVRLLR RLMGVRLRMT GREHLPPAGR
     SLVLVANHQS YLDALALIEA VPRPMRFVAK RELNANPLAG RFLERLGTLF VERFDLQQSH
     REGERLQTAL RDGASLAFFP EGTFRERPGL LPFRMGAFVA AAEAGVPILP VTIRGTRAVM
     PGDRFRPRPG TIEVVIAAPI LPQGTDWEAA SLLRDAARAV IAARDAA
//
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