ACPS_MYCMM
ID ACPS_MYCMM Reviewed; 130 AA.
AC B2HPL7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=MMAR_3961;
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=216594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(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}.
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DR EMBL; CP000854; ACC42369.1; -; Genomic_DNA.
DR RefSeq; WP_011741517.1; NC_010612.1.
DR AlphaFoldDB; B2HPL7; -.
DR SMR; B2HPL7; -.
DR STRING; 216594.MMAR_3961; -.
DR EnsemblBacteria; ACC42369; ACC42369; MMAR_3961.
DR GeneID; 64262515; -.
DR KEGG; mmi:MMAR_3961; -.
DR eggNOG; COG0736; Bacteria.
DR HOGENOM; CLU_089696_2_0_11; -.
DR OMA; NTCGLGH; -.
DR OrthoDB; 1893660at2; -.
DR Proteomes; UP000001190; 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; 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..130
FT /note="Holo-[acyl-carrier-protein] synthase"
FT /id="PRO_1000093897"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
SQ SEQUENCE 130 AA; 13968 MW; E373237850DF89A5 CRC64;
MGIVGVGIDL VSIPDFAEQV DQPGTAFAAT FTPGERRDAS DKSSSAARHL AARWAAKEAV
IKAWSGSRFA QRPVLPEDIH RDIEVVTDMW GRPRVRLTGE IAKHLADVTI HVSLTHEGDT
AAAVAILETS