位置:首页 > 蛋白库 > AAS_CROS8
AAS_CROS8
ID   AAS_CROS8               Reviewed;         719 AA.
AC   A7MR36;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Bifunctional protein Aas {ECO:0000255|HAMAP-Rule:MF_01162};
DE   Includes:
DE     RecName: Full=2-acylglycerophosphoethanolamine acyltransferase {ECO:0000255|HAMAP-Rule:MF_01162};
DE              EC=2.3.1.40 {ECO:0000255|HAMAP-Rule:MF_01162};
DE     AltName: Full=2-acyl-GPE acyltransferase {ECO:0000255|HAMAP-Rule:MF_01162};
DE     AltName: Full=Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01162};
DE   Includes:
DE     RecName: Full=Acyl-[acyl-carrier-protein] synthetase {ECO:0000255|HAMAP-Rule:MF_01162};
DE              EC=6.2.1.20 {ECO:0000255|HAMAP-Rule:MF_01162};
DE     AltName: Full=Acyl-ACP synthetase {ECO:0000255|HAMAP-Rule:MF_01162};
DE     AltName: Full=Long-chain-fatty-acid--[acyl-carrier-protein] ligase {ECO:0000255|HAMAP-Rule:MF_01162};
GN   Name=aas {ECO:0000255|HAMAP-Rule:MF_01162}; OrderedLocusNames=ESA_00472;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
CC   -!- FUNCTION: Plays a role in lysophospholipid acylation. Transfers fatty
CC       acids to the 1-position via an enzyme-bound acyl-ACP intermediate in
CC       the presence of ATP and magnesium. Its physiological function is to
CC       regenerate phosphatidylethanolamine from 2-acyl-glycero-3-
CC       phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or
CC       degradation by phospholipase A1. {ECO:0000255|HAMAP-Rule:MF_01162}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP]
CC         = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP];
CC         Xref=Rhea:RHEA:10304, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:14125,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:64612, ChEBI:CHEBI:65213,
CC         ChEBI:CHEBI:138651; EC=2.3.1.40; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01162};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acid + ATP + holo-[ACP] = a long-chain
CC         fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:45588,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57560, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:133243, ChEBI:CHEBI:456215; EC=6.2.1.20;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01162};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01162}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01162}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the 2-acyl-GPE
CC       acetyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01162}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the ATP-dependent
CC       AMP-binding enzyme family. {ECO:0000255|HAMAP-Rule:MF_01162}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000783; ABU75767.1; -; Genomic_DNA.
DR   RefSeq; WP_012123884.1; NC_009778.1.
DR   AlphaFoldDB; A7MR36; -.
DR   SMR; A7MR36; -.
DR   PRIDE; A7MR36; -.
DR   EnsemblBacteria; ABU75767; ABU75767; ESA_00472.
DR   KEGG; esa:ESA_00472; -.
DR   PATRIC; fig|290339.8.peg.428; -.
DR   HOGENOM; CLU_000022_59_8_6; -.
DR   OMA; ANWVYLE; -.
DR   OrthoDB; 961884at2; -.
DR   Proteomes; UP000000260; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008779; F:acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   HAMAP; MF_01162; Aas; 1.
DR   InterPro; IPR023775; Aas.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SMART; SM00563; PlsC; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; ATP-binding; Cell inner membrane; Cell membrane; Ligase;
KW   Membrane; Multifunctional enzyme; Nucleotide-binding; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..719
FT                   /note="Bifunctional protein Aas"
FT                   /id="PRO_1000065640"
FT   TRANSMEM        258..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01162"
FT   TRANSMEM        409..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01162"
FT   REGION          15..138
FT                   /note="Acyltransferase"
FT   REGION          233..646
FT                   /note="AMP-binding"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01162"
SQ   SEQUENCE   719 AA;  79978 MW;  215C25A312722834 CRC64;
     MVLKFFRWLF RLLFRIQVYG DTGPLTQQRV LITPNHVSFL DGALMALFLP VRPVFAVYTS
     ISQQWYMRAL KPLIDFVPLD PTKPMSVKQL VRLVGEGRPV VIFPEGRISI SGSLMKIYEG
     AGFVAAKSQA TVIPVRIEGA ELTFFSRLKG LVKRRLFPRI SIHILPPTSI PMPDAPKARD
     RRKMAGEMLH QVMMEARMAA RPRETLFEAL INAQKRYGES KSCLEDINFK PDTYRSLMMK
     TLFVGRILDK YSAPREAIGL MLPNASISAA VIFGAVMRGR IPAMMNYTAG VQGLTSAITA
     AQIKTIFTSR QFLDKGKLWH LSEQITSVRW VFLEDLKGEV TAKDKAWIFA HLLMPRLAQV
     EQQPEDAALI LFTSGSEGNP KGVVHSHKSL LANVEQIRTI ADFTADDKFM SALPLFHSFG
     LTVGLFTPLL TGAEVFLYPS PLHYRVVPEL VYDRNCTVIF GTSTFLGHYA RFAHPYDFHL
     VRYVVAGAEK LQESTKQIWQ DKFGLRILEG YGVTECAPVV SINVPMAAKP GTVGRILPAM
     DARLVEVPGI EQGGRLQLKG PNIMKGYLRV ENPGVLEAPA AENPQGVSEP GWYDTGDIVA
     FDEQGFVQIQ GRAKRFAKIA GEMVSLEMVE SLALAVSPEK MHATAIKHDA AKGEALVLFT
     TDPELTREKL AQQARSKGVP ELAVPRDIRF LKQLPLLGSG KPDFVSLKKL VDQEETHHA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024