ACPS_BLOPB
ID ACPS_BLOPB Reviewed; 125 AA.
AC Q492D3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=BPEN_558;
OS Blochmannia pennsylvanicus (strain BPEN).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=291272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPEN;
RX PubMed=16077009; DOI=10.1101/gr.3771305;
RA Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT evolutionary trends among bacterial mutualists of insects.";
RL Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ41168.1; -; Genomic_DNA.
DR AlphaFoldDB; Q492D3; -.
DR SMR; Q492D3; -.
DR STRING; 291272.BPEN_558; -.
DR EnsemblBacteria; AAZ41168; AAZ41168; BPEN_558.
DR KEGG; bpn:BPEN_558; -.
DR eggNOG; COG0736; Bacteria.
DR HOGENOM; CLU_089696_3_1_6; -.
DR OMA; DERHYAV; -.
DR BioCyc; CBLO291272:BPEN_RS02755-MON; -.
DR Proteomes; UP000007794; 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 Transferase.
FT CHAIN 1..125
FT /note="Holo-[acyl-carrier-protein] synthase"
FT /id="PRO_0000228270"
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 125 AA; 14080 MW; 9681F3CFE59FC31A CRC64;
MIHGIGIDIV DIRKIKKIIT HSGDKLATRI LSKSEWKIYK NKKHPVHFLA KRFAAKEAVS
KAFGTGINQG VTFNQIEIFN DKLGKPMLHL FSCTALLANK LSLKKMHITL SDTNSYACAF
VILER
