(data stored in SCRATCH zone)

SWISSPROT: Q4ZZA5_PSEU2

ID   Q4ZZA5_PSEU2            Unreviewed;       213 AA.
AC   Q4ZZA5;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Phosphoribosyl-dephospho-CoA transferase {ECO:0000256|HAMAP-Rule:MF_00650};
DE            EC=2.7.7.66 {ECO:0000256|HAMAP-Rule:MF_00650};
DE   AltName: Full=Malonate decarboxylase holo-[acyl-carrier-protein] synthase {ECO:0000256|HAMAP-Rule:MF_00650};
DE            Short=Holo-ACP synthase {ECO:0000256|HAMAP-Rule:MF_00650};
GN   Name=mdcG {ECO:0000256|HAMAP-Rule:MF_00650};
GN   OrderedLocusNames=Psyr_0447 {ECO:0000313|EMBL:AAY35517.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35517.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35517.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35517.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- FUNCTION: Transfers 2'-(5-triphosphoribosyl)-3'-dephosphocoenzyme-
CC       A to the apo-[acyl-carrier-protein] of the malonate decarboxylase
CC       to yield holo-[acyl-carrier-protein]. {ECO:0000256|HAMAP-
CC       Rule:MF_00650}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA +
CC         apo-[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:0000256|HAMAP-Rule:MF_00650};
CC   -!- SIMILARITY: Belongs to the MdcG family. {ECO:0000256|HAMAP-
CC       Rule:MF_00650}.
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DR   EMBL; CP000075; AAY35517.1; -; Genomic_DNA.
DR   RefSeq; WP_011266410.1; NC_007005.1.
DR   RefSeq; YP_233555.1; NC_007005.1.
DR   STRING; 205918.Psyr_0447; -.
DR   EnsemblBacteria; AAY35517; AAY35517; Psyr_0447.
DR   GeneID; 3365923; -.
DR   KEGG; psb:Psyr_0447; -.
DR   PATRIC; fig|205918.7.peg.464; -.
DR   eggNOG; ENOG4105PSI; Bacteria.
DR   eggNOG; ENOG4111V8X; LUCA.
DR   HOGENOM; HOG000080652; -.
DR   KO; K13934; -.
DR   OMA; RIPVGVR; -.
DR   BioCyc; PSYR205918:G1G4J-448-MONOMER; -.
DR   Proteomes; UP000000426; 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;
DR   PRODOM; Q4ZZA5.
DR   SWISS-2DPAGE; Q4ZZA5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00650};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00650}.
FT   ACT_SITE    138    138       {ECO:0000256|HAMAP-Rule:MF_00650}.
FT   ACT_SITE    140    140       {ECO:0000256|HAMAP-Rule:MF_00650}.
SQ   SEQUENCE   213 AA;  23079 MW;  AB0E03F40FFD5598 CRC64;
     MVISNTGAVL PHDLLWGMPL TALPDDAPKW AVEAVLAGQP VVVRRQAMPA GQQVAVGLRG
     RGREQRYAAS MPLAEVCRRV MPEQLIDAPT EIHQQWPALQ ALRQIRPVME ALELDWGVGG
     SAGFELASGI AALHQDSDLD LILRTPGRLN RRCAAELVEA LETSVCRVDV QLQLESGAVA
     LREWARPTGR VLLKTATGAR LVADPWHLGQ VCA
//

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