MDCG_XANCB
ID MDCG_XANCB Reviewed; 213 AA.
AC B0RN93;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 62.
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};
GN OrderedLocusNames=xcc-b100_0593;
OS Xanthomonas campestris pv. campestris (strain B100).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=509169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B100;
RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA Puehler A.;
RT "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT the reconstruction of metabolic pathways involved in xanthan
RT biosynthesis.";
RL J. Biotechnol. 134:33-45(2008).
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; AM920689; CAP49928.1; -; Genomic_DNA.
DR AlphaFoldDB; B0RN93; -.
DR KEGG; xca:xcc-b100_0593; -.
DR HOGENOM; CLU_075747_0_1_6; -.
DR OMA; GGVNWRE; -.
DR Proteomes; UP000001188; 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..213
FT /note="Phosphoribosyl-dephospho-CoA transferase"
FT /id="PRO_1000130988"
FT ACT_SITE 135
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00650"
FT ACT_SITE 137
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00650"
SQ SEQUENCE 213 AA; 22901 MW; C784E3CD7B061AEF CRC64;
MAGRHALVWL RADAPSQALT PGAQPRLQAW FAAGFPAVVA RRDGAEQPGQ VRLGVPLPPA
QGKQRIALCA QVSDIARSVP ALALPEVISH APPQWQAALH ALQAQATAIG MQPRVFGSFA
FQAVTGLPYV HAASDVDLLW TLDTPTQAHA VVTLLQQWEH VTARRADGEL LLPDGNAVNW
REYAGDAQQV LVKRNDGCRL LPRTALFPER CAA