MDCB_AZOVD
ID MDCB_AZOVD Reviewed; 292 AA.
AC C1DNP5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=Avin_10290;
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: 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; CP001157; ACO77261.1; -; Genomic_DNA.
DR RefSeq; WP_012699684.1; NC_012560.1.
DR AlphaFoldDB; C1DNP5; -.
DR STRING; 322710.Avin_10290; -.
DR EnsemblBacteria; ACO77261; ACO77261; Avin_10290.
DR KEGG; avn:Avin_10290; -.
DR eggNOG; COG1767; Bacteria.
DR HOGENOM; CLU_056179_0_0_6; -.
DR OMA; QSWQRPA; -.
DR OrthoDB; 1738403at2; -.
DR Proteomes; UP000002424; 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..292
FT /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT dephosphocoenzyme-A synthase"
FT /id="PRO_1000205872"
SQ SEQUENCE 292 AA; 31203 MW; BBDF34F9FEDAF7DB CRC64;
MSAFIATIPR PSLAERFADL AVGALIDEAE LSPKPALVDR RGSGAHRDLD LKLMHASARA
LWPAFHAMAE AARSLAELDR PLRETIGRLG REGEARMLAV TGGVNTHRGA IWALGLLVTA
AALEPQRLAP EQVSLRAARL ARLEDRQMPA QPPSHGERVR QRYGVRGARE EARGGFPGVI
RHGLPQLRRS RAAGCDENHA RLDALLAIMA QLEDTCVLHR AGLEGLRCMQ DGARAVLVAG
GSASLAGRRS LRDLELGLLE LNASPGGAAD LLAVTLFLDR LEPMLGAPIG SL
