位置:首页 > 蛋白库 > ACPS_METEP
ACPS_METEP
ID   ACPS_METEP              Reviewed;         136 AA.
AC   A9W511;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Holo-[acyl-carrier-protein] synthase {ECO:0000255|HAMAP-Rule:MF_00101};
DE            Short=Holo-ACP synthase {ECO:0000255|HAMAP-Rule:MF_00101};
DE            EC=2.7.8.7 {ECO:0000255|HAMAP-Rule:MF_00101};
DE   AltName: Full=4'-phosphopantetheinyl transferase AcpS {ECO:0000255|HAMAP-Rule:MF_00101};
GN   Name=acpS {ECO:0000255|HAMAP-Rule:MF_00101}; OrderedLocusNames=Mext_2272;
OS   Methylorubrum extorquens (strain PA1) (Methylobacterium extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=419610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Marx C., Richardson P.;
RT   "Complete sequence of Methylobacterium extorquens PA1.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme A to
CC       a Ser of acyl-carrier-protein. {ECO:0000255|HAMAP-Rule:MF_00101}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-
CC         [ACP]; Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC         COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; EC=2.7.8.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00101};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00101};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00101}.
CC   -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family.
CC       {ECO:0000255|HAMAP-Rule:MF_00101}.
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; CP000908; ABY30667.1; -; Genomic_DNA.
DR   RefSeq; WP_012253716.1; NC_010172.1.
DR   AlphaFoldDB; A9W511; -.
DR   SMR; A9W511; -.
DR   STRING; 419610.Mext_2272; -.
DR   EnsemblBacteria; ABY30667; ABY30667; Mext_2272.
DR   KEGG; mex:Mext_2272; -.
DR   eggNOG; COG0736; Bacteria.
DR   HOGENOM; CLU_089696_0_2_5; -.
DR   OMA; DERHYAV; -.
DR   BioCyc; MEXT419610:MEXT_RS11455-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.470.20; -; 1.
DR   HAMAP; MF_00101; AcpS; 1.
DR   InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR   InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR   InterPro; IPR002582; ACPS.
DR   InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR   Pfam; PF01648; ACPS; 1.
DR   SUPFAM; SSF56214; SSF56214; 1.
DR   TIGRFAMs; TIGR00516; acpS; 1.
DR   TIGRFAMs; TIGR00556; pantethn_trn; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW   Transferase.
FT   CHAIN           1..136
FT                   /note="Holo-[acyl-carrier-protein] synthase"
FT                   /id="PRO_1000093893"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
FT   BINDING         57
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
SQ   SEQUENCE   136 AA;  14840 MW;  FFF68414D6254A3A CRC64;
     MILGIGTDLC DIRRIESSLE RFGDRFTHRV FTDGERGKCD QRAARGPSYA RRFAAKEACA
     KALGTGMSQG VFWRDMEVVN LPSGQPTLNL TGGAREQLAR MVPAGHEARL HLTLTDEPPL
     AQAFVIIEAV PITATS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024