(data stored in ACNUC7421 zone)

SWISSPROT: D6XXZ1_BACIE

ID   D6XXZ1_BACIE            Unreviewed;       131 AA.
AC   D6XXZ1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Holo-[acyl-carrier-protein] synthase {ECO:0000256|HAMAP-Rule:MF_00101};
DE            Short=Holo-ACP synthase {ECO:0000256|HAMAP-Rule:MF_00101};
DE            EC=2.7.8.7 {ECO:0000256|HAMAP-Rule:MF_00101};
DE   AltName: Full=4'-phosphopantetheinyl transferase AcpS {ECO:0000256|HAMAP-Rule:MF_00101};
GN   Name=acpS {ECO:0000256|HAMAP-Rule:MF_00101};
GN   OrderedLocusNames=Bsel_0528 {ECO:0000313|EMBL:ADH98064.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98064.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH98064.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) 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:0000256|HAMAP-
CC       Rule:MF_00101, ECO:0000256|SAAS:SAAS01153667}.
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:0000256|HAMAP-Rule:MF_00101,
CC         ECO:0000256|SAAS:SAAS01144854};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00101, ECO:0000256|SAAS:SAAS01153678};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00101,
CC       ECO:0000256|SAAS:SAAS01153709}.
CC   -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS
CC       family. {ECO:0000256|HAMAP-Rule:MF_00101,
CC       ECO:0000256|SAAS:SAAS01153685}.
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DR   EMBL; CP001791; ADH98064.1; -; Genomic_DNA.
DR   RefSeq; WP_013171493.1; NC_014219.1.
DR   STRING; 439292.Bsel_0528; -.
DR   EnsemblBacteria; ADH98064; ADH98064; Bsel_0528.
DR   KEGG; bse:Bsel_0528; -.
DR   eggNOG; ENOG41081XD; Bacteria.
DR   eggNOG; COG0736; LUCA.
DR   HOGENOM; HOG000014315; -.
DR   KO; K00997; -.
DR   OMA; DERHYAV; -.
DR   OrthoDB; 1893660at2; -.
DR   BioCyc; BSEL439292:G1GLR-556-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
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; D6XXZ1.
DR   SWISS-2DPAGE; D6XXZ1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00101,
KW   ECO:0000256|SAAS:SAAS01153712};
KW   Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00101,
KW   ECO:0000256|SAAS:SAAS00089117};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_00101,
KW   ECO:0000256|SAAS:SAAS00089144};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00101,
KW   ECO:0000256|SAAS:SAAS00089157};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00101,
KW   ECO:0000256|SAAS:SAAS00089094};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00101,
KW   ECO:0000256|SAAS:SAAS01077217};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00101,
KW   ECO:0000256|SAAS:SAAS01077211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00101,
KW   ECO:0000256|SAAS:SAAS00071051}.
FT   DOMAIN        4    104       ACPS. {ECO:0000259|Pfam:PF01648}.
FT   METAL         8      8       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00101}.
FT   METAL        59     59       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00101}.
SQ   SEQUENCE   131 AA;  14622 MW;  16A851C14AD59754 CRC64;
     MIQGIGLDII ELERIRRLTV RQPRFSARIL TERELTKMAS FTDANRKIEY LAGRYAAKEA
     FSKALGCGIG GELSFQDIDI INREDGRPEL FCQALDQDTR ALVSITHTRD MAAAQVILER
     SPGPLNDKSG V
//

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