MDCB_PSEAE
ID MDCB_PSEAE Reviewed; 293 AA.
AC Q9I6S9;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=PA0209;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG03598.1; -; Genomic_DNA.
DR PIR; F83618; F83618.
DR RefSeq; NP_248900.1; NC_002516.2.
DR RefSeq; WP_003112667.1; NZ_QZGE01000024.1.
DR AlphaFoldDB; Q9I6S9; -.
DR STRING; 287.DR97_3166; -.
DR PaxDb; Q9I6S9; -.
DR PRIDE; Q9I6S9; -.
DR EnsemblBacteria; AAG03598; AAG03598; PA0209.
DR GeneID; 879248; -.
DR KEGG; pae:PA0209; -.
DR PATRIC; fig|208964.12.peg.217; -.
DR PseudoCAP; PA0209; -.
DR HOGENOM; CLU_056179_0_0_6; -.
DR InParanoid; Q9I6S9; -.
DR OMA; QSWQRPA; -.
DR PhylomeDB; Q9I6S9; -.
DR BioCyc; PAER208964:G1FZ6-211-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR GO; GO:0051191; P:prosthetic group biosynthetic process; IBA:GO_Central.
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; Reference proteome; Transferase.
FT CHAIN 1..293
FT /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT dephosphocoenzyme-A synthase"
FT /id="PRO_0000214673"
SQ SEQUENCE 293 AA; 30534 MW; A9A085F070C680B3 CRC64;
MNAIANLAAT PGADLGECLA DLAVDALIDE AELSPKPALV DRRGNGAHAD LHLGLMQASA
LSLWPCFKEM ADAAQRHGRI DARLRGVLGQ LGRDGEAAML RTTEGVNTHR GAIWALGLLV
AAAALEPRRT QAGEVAARAG RIALLDDPAA AIGDSHGERV RRRYGVGGAR EEARLCFPRA
VRHGLPQLWR SREGGAGEQN ARLDALLAIM SVLDDTCVLH RAGRVGLAAM QDGARAVLAA
GGSASLAGRR RLCELDRRLL ALNASPGGAA DLLAACLFLD RLPAVSGGWA GSL
