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Database: UniProt/TrEMBL
Entry: I3Y9V3_THIV6
LinkDB: I3Y9V3_THIV6
Original site: I3Y9V3_THIV6 
ID   I3Y9V3_THIV6            Unreviewed;       929 AA.
AC   I3Y9V3;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   30-AUG-2017, entry version 29.
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=Thivi_1799 {ECO:0000313|EMBL:AFL73771.1};
OS   Thiocystis violascens (strain ATCC 17096 / DSM 198 / 6111) (Chromatium
OS   violascens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Chromatiaceae; Thiocystis.
OX   NCBI_TaxID=765911 {ECO:0000313|EMBL:AFL73771.1, ECO:0000313|Proteomes:UP000006062};
RN   [1] {ECO:0000313|EMBL:AFL73771.1, ECO:0000313|Proteomes:UP000006062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17096 / DSM 198 / 6111
RC   {ECO:0000313|Proteomes:UP000006062};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K.,
RA   Liu Z., Frigaard N.-U., Bryant D., Woyke T.;
RT   "Complete sequence of Thiocystis violascens DSM 198.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003154; AFL73771.1; -; Genomic_DNA.
DR   RefSeq; WP_014778231.1; NC_018012.1.
DR   ProteinModelPortal; I3Y9V3; -.
DR   EnsemblBacteria; AFL73771; AFL73771; Thivi_1799.
DR   KEGG; tvi:Thivi_1799; -.
DR   OMA; VPVDFMS; -.
DR   OrthoDB; POG091H0HAF; -.
DR   BioCyc; TVIO765911:GLMH-1700-MONOMER; -.
DR   Proteomes; UP000006062; 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:AFL73771.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006062};
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:UP000006062};
KW   Transferase {ECO:0000256|RuleBase:RU361267,
KW   ECO:0000313|EMBL:AFL73771.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    326    349       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    693    712       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       43     85       Carrier. {ECO:0000259|PROSITE:PS50075}.
FT   MOD_RES      50     50       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00258}.
SQ   SEQUENCE   929 AA;  101704 MW;  A74CEA4C7272CA0D CRC64;
     MNDSMQAADQ ESRLLSILQA FARESRLPEP PEGIGLDTRL ETDLGLDSLS RSELIARVEA
     GLGVHLRDEA LLAATARDLL GLARAGAGLT GTVAAAPTMT TRRGAGIPTE ALTLPDALLW
     HGERHGSRIH ITYYDSDDQA HPITYADLIK GASQVAGRLK QAGLSVGGTV AIMLPTGPEY
     FFGFFGILAA GGVPVPIYPP ARPQQIEDHL RRHARILDNA GTTILITVPE ARAVARLLRL
     QVASLREIIT LEGLDAEAPE TNWARPDPQD IAFLQYTSGS TGDPKGVVLS HADLLANIRA
     MGEAVAIGPD DVFVSWLPLY HDMGLIGAWL GSLYFGIPLI SMSPLAFLAR PRRWLQAIHR
     HRGTLSAAPN FAYELCLARL SDAQLDGLDL GSWRRAFNGA EPVSAQTLRR FAERFAPYGL
     RPDALAPVYG LAEAAVGLAF PPADLGPRID CIDRARFASS GYALPVGCDD PEAMDVVACG
     RALPGYRVRI VDETGGERPE RHEGLLQFQG PSATRGYYRN PEATARLIRD GWHETGDRAY
     LAGGDIHLTG RVKDLIIRGG RNLYPYEVEQ ALGELPGVRK GCVVAFAALD PKQGSERLVI
     VAESKERDPA RRRALMQRMR ERATDILGLP PDEIVLAPPR SVLKTSSGKL RRGDMRARYL
     AGNLLEGPSR PLWQLVRVGG SAFMSRLRRL PGTLYAGYAW TIFYLIAPWF WIATMLAPRL
     HWRWTLLRFG IRLLRRLAFV RLTVMGREHI PPPGSPYVLV ANHQSYLDAL ALIETFEQPI
     RFVAKRELMR NPLVGRFLAR MGTFFVDRFD LQRSGSESAR IGEALAHGAT LGFFPEGTFR
     EQPGLLPFRM GAFAAAAQAG VPVVPVTLVG TRELMPGDRF KPRPGQAQAV IGPPLMPAGN
     DWGSAVELRD AARAEIAEQL ERHERTRLL
//
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