MDCG_AZOVD
ID MDCG_AZOVD Reviewed; 212 AA.
AC C1DNP9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Phosphoribosyl-dephospho-CoA transferase {ECO:0000255|HAMAP-Rule:MF_00650};
DE EC=2.7.7.66 {ECO:0000255|HAMAP-Rule:MF_00650};
DE AltName: Full=Malonate decarboxylase holo-[acyl-carrier-protein] synthase {ECO:0000255|HAMAP-Rule:MF_00650};
DE Short=Holo-ACP synthase {ECO:0000255|HAMAP-Rule:MF_00650};
GN Name=mdcG {ECO:0000255|HAMAP-Rule:MF_00650}; OrderedLocusNames=Avin_10330;
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303;
RX PubMed=19429624; DOI=10.1128/jb.00504-09;
RA Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
CC -!- FUNCTION: Transfers 2'-(5-triphosphoribosyl)-3'-dephosphocoenzyme-A to
CC the apo-[acyl-carrier-protein] of the malonate decarboxylase to yield
CC holo-[acyl-carrier-protein]. {ECO:0000255|HAMAP-Rule:MF_00650}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + apo-
CC [malonate decarboxylase ACP] = diphosphate + holo-[malonate
CC decarboxylase ACP]; Xref=Rhea:RHEA:42644, Rhea:RHEA-COMP:10160,
CC Rhea:RHEA-COMP:10161, ChEBI:CHEBI:29999, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61378, ChEBI:CHEBI:82683; EC=2.7.7.66;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00650};
CC -!- SIMILARITY: Belongs to the MdcG family. {ECO:0000255|HAMAP-
CC Rule:MF_00650}.
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DR EMBL; CP001157; ACO77265.1; -; Genomic_DNA.
DR RefSeq; WP_012699688.1; NC_012560.1.
DR AlphaFoldDB; C1DNP9; -.
DR STRING; 322710.Avin_10330; -.
DR EnsemblBacteria; ACO77265; ACO77265; Avin_10330.
DR KEGG; avn:Avin_10330; -.
DR eggNOG; ENOG502Z8NU; Bacteria.
DR HOGENOM; CLU_111981_0_0_6; -.
DR OMA; PHDLLWG; -.
DR OrthoDB; 1409077at2; -.
DR Proteomes; UP000002424; Chromosome.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00650; Malonate_MdcG; 1.
DR InterPro; IPR017557; Holo-ACP_synthase.
DR Pfam; PF10620; MdcG; 1.
DR TIGRFAMs; TIGR03135; malonate_mdcG; 1.
PE 3: Inferred from homology;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..212
FT /note="Phosphoribosyl-dephospho-CoA transferase"
FT /id="PRO_1000212404"
FT ACT_SITE 139
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00650"
FT ACT_SITE 141
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00650"
SQ SEQUENCE 212 AA; 23019 MW; 9CC72E167DA3C618 CRC64;
MHETRLLPQP HDLLWGMSTD RLDAAAPTWA AEVLAAGRPV VVRRAPARDG WIAVGVRGHG
REQRHAAWMP RAAIRRRVQP EQLTGGGERE GVCAPLRALA LLQPQLDALC RQRGLAWGVT
GGAGYQLATG VTVLGEHSDL DLLLRVPRPL ERRQALALLE RLEQLPCRVD LQLETPAGAV
ALRDWASPAA RVLLKAGSGA RLVGDPWREV AA
