(data stored in ACNUC7421 zone)

SWISSPROT: ACPS_PARDP

ID   ACPS_PARDP              Reviewed;         139 AA.
AC   A1AZ41;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 77.
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};
GN   OrderedLocusNames=Pden_0421;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme
CC       A to a Ser of acyl-carrier-protein. {ECO:0000255|HAMAP-
CC       Rule:MF_00101}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) +
CC         holo-[ACP]; Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685,
CC         Rhea:RHEA-COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:58343, ChEBI:CHEBI:64479;
CC         EC=2.7.8.7; 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
CC       family. {ECO:0000255|HAMAP-Rule:MF_00101}.
DR   EMBL; CP000489; ABL68535.1; -; Genomic_DNA.
DR   RefSeq; WP_011746768.1; NC_008686.1.
DR   SMR; A1AZ41; -.
DR   STRING; 318586.Pden_0421; -.
DR   PRIDE; A1AZ41; -.
DR   EnsemblBacteria; ABL68535; ABL68535; Pden_0421.
DR   KEGG; pde:Pden_0421; -.
DR   eggNOG; ENOG4105KJV; Bacteria.
DR   eggNOG; COG0736; LUCA.
DR   HOGENOM; HOG000014316; -.
DR   KO; K00997; -.
DR   OMA; DERHYAV; -.
DR   BioCyc; PDEN318586:G1GW1-421-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
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   ProDom; PD004282; PPantethiene-prot_Trfase; 1.
DR   SUPFAM; SSF56214; SSF56214; 1.
DR   TIGRFAMs; TIGR00516; acpS; 1.
DR   TIGRFAMs; TIGR00556; pantethn_trn; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1AZ41.
DR   SWISS-2DPAGE; A1AZ41.
KW   Complete proteome; Cytoplasm; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW   Magnesium; Metal-binding; Reference proteome; Transferase.
FT   CHAIN         1    139       Holo-[acyl-carrier-protein] synthase.
FT                                /FTId=PRO_1000008469.
FT   METAL         8      8       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00101}.
FT   METAL        57     57       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00101}.
SQ   SEQUENCE   139 AA;  15133 MW;  65319F912D3F3B56 CRC64;
     MILGIGSDLC NIDRIAGVLE RHGDRFRRRV FTETELALAG RRRHEAATLA KRWAAKEACS
     KALGTGLAMG ISWKDMAVRN LRGGQPTMEL TGWAAERLAA MTPPGHRAHV HVTLTDDHPW
     AQAFVVIEAL PDDAQAGTA
//

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