MDCB_PSE14
ID MDCB_PSE14 Reviewed; 291 AA.
AC Q48PD2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=PSPPH_0434;
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6;
RX PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA Buell R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ35650.1; -; Genomic_DNA.
DR RefSeq; WP_004666473.1; NC_005773.3.
DR AlphaFoldDB; Q48PD2; -.
DR STRING; 264730.PSPPH_0434; -.
DR EnsemblBacteria; AAZ35650; AAZ35650; PSPPH_0434.
DR KEGG; psp:PSPPH_0434; -.
DR eggNOG; COG1767; Bacteria.
DR HOGENOM; CLU_056179_0_0_6; -.
DR OMA; QSWQRPA; -.
DR OrthoDB; 1738403at2; -.
DR Proteomes; UP000000551; 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..291
FT /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT dephosphocoenzyme-A synthase"
FT /id="PRO_1000189590"
SQ SEQUENCE 291 AA; 30487 MW; EE381AB6929530BA CRC64;
MSALQLTPQA ASLAERLADL AVDALIAEAD LSPKPALVDR RGSGAHTDLH LGLMHSSALS
LWPTFKLMAD AAGQFNTVGQ PLREALGRLG RDGEATMLRT TQGVNTHRGA IWALGLLVTA
AALDARNCAP EAVLARAASL AQIKDRQVLV QGSHGNEVVR RYGVMGAREQ AQQGFPAVRD
FALPQLQRSR AAGSGEQNAR LDALLAIMTT LSDTCVLHRA GIEGLHTMQR GAQHVLDVGG
SASLAGRRAL NQLDQQLLAL NASPGGAADL LAACLFIDGL EPALGRVSRS V
