ACPS_KINRD
ID ACPS_KINRD Reviewed; 117 AA.
AC A6W5X5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Krad_0725;
OS Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae; Kineococcus.
OX NCBI_TaxID=266940;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216;
RX PubMed=19057647; DOI=10.1371/journal.pone.0003878;
RA Bagwell C.E., Bhat S., Hawkins G.M., Smith B.W., Biswas T., Hoover T.R.,
RA Saunders E., Han C.S., Tsodikov O.V., Shimkets L.J.;
RT "Survival in nuclear waste, extreme resistance, and potential applications
RT gleaned from the genome sequence of Kineococcus radiotolerans SRS30216.";
RL PLoS ONE 3:e3878-e3878(2008).
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; CP000750; ABS02214.1; -; Genomic_DNA.
DR RefSeq; WP_012084939.1; NC_009664.2.
DR AlphaFoldDB; A6W5X5; -.
DR SMR; A6W5X5; -.
DR STRING; 266940.Krad_0725; -.
DR EnsemblBacteria; ABS02214; ABS02214; Krad_0725.
DR KEGG; kra:Krad_0725; -.
DR eggNOG; COG0736; Bacteria.
DR HOGENOM; CLU_089696_0_0_11; -.
DR OMA; LGVRSWH; -.
DR OrthoDB; 1893660at2; -.
DR Proteomes; UP000001116; 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 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 Reference proteome; Transferase.
FT CHAIN 1..117
FT /note="Holo-[acyl-carrier-protein] synthase"
FT /id="PRO_1000075643"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
SQ SEQUENCE 117 AA; 12524 MW; 73D03790F0752EC6 CRC64;
MIIGVGIDVV DVARFKRQVE RTPLLLERLF GDGERNLPAE SLAARFAAKE AVAKSLGAPV
GLVWRDVVVE REDGHRPEIA VRGSAKKIAD EAGVAVFHLS LSHDAGIATA MVVAESR
