MDCB_PSEPF
ID MDCB_PSEPF Reviewed; 290 AA.
AC Q3K5B6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Probable 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase {ECO:0000255|HAMAP-Rule:MF_01883};
DE Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase {ECO:0000255|HAMAP-Rule:MF_01883};
DE EC=2.4.2.52 {ECO:0000255|HAMAP-Rule:MF_01883};
GN Name=mdcB {ECO:0000255|HAMAP-Rule:MF_01883}; OrderedLocusNames=Pfl01_5301;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
CC -!- FUNCTION: Involved in the formation of 2-(5''-phosphoribosyl)-3'-
CC dephosphocoenzyme-A, the prosthetic group of the acyl-carrier protein
CC of the malonate decarboxylase. {ECO:0000255|HAMAP-Rule:MF_01883}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-dephospho-CoA + ATP = 2'-(5''-triphospho-alpha-D-ribosyl)-
CC 3'-dephospho-CoA + adenine; Xref=Rhea:RHEA:15117, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57328, ChEBI:CHEBI:61378; EC=2.4.2.52;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01883};
CC -!- SIMILARITY: Belongs to the CitG/MdcB family. {ECO:0000255|HAMAP-
CC Rule:MF_01883}.
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DR EMBL; CP000094; ABA77038.1; -; Genomic_DNA.
DR RefSeq; WP_011336359.1; NC_007492.2.
DR AlphaFoldDB; Q3K5B6; -.
DR STRING; 205922.Pfl01_5301; -.
DR EnsemblBacteria; ABA77038; ABA77038; Pfl01_5301.
DR KEGG; pfo:Pfl01_5301; -.
DR eggNOG; COG1767; Bacteria.
DR HOGENOM; CLU_056179_0_0_6; -.
DR OMA; QSWQRPA; -.
DR Proteomes; UP000002704; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR HAMAP; MF_01883; MdcB; 1.
DR InterPro; IPR002736; CitG.
DR InterPro; IPR017555; TriPribosyl-deP-CoA_syn.
DR PANTHER; PTHR30201; PTHR30201; 1.
DR Pfam; PF01874; CitG; 1.
DR TIGRFAMs; TIGR03132; malonate_mdcB; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding; Transferase.
FT CHAIN 1..290
FT /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT dephosphocoenzyme-A synthase"
FT /id="PRO_0000255404"
SQ SEQUENCE 290 AA; 30649 MW; 1E7C48FBFAFB0D9F CRC64;
MHALNLQPKT ITLAERLADL AVDALIDEAD LSPKPALVDR RGNGAHTDLH LGLMHASALA
LWPAFKEMAE AALEFGEIGL PLREAIGRIG REGEQAMLAT THGVNTHRGA IWALGLLVTA
AALDTKSTSA GAVTLRAARL ALLDDRYAPR PLSHGAQVAQ RYGARGAREE AQLGFPSVVQ
RGLPQLKRSR AAGHGEQNAR LDALLAIMTD LADTCVLYRA GEQGLHAMQH GARAVLDAGG
SASLTGRRRL HELDQQLIAL NASPGGAADL LAASLLLDRI ERDGILQGAF
