(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZK12_PSEAB

ID   A0A0H2ZK12_PSEAB        Unreviewed;       230 AA.
AC   A0A0H2ZK12;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   05-JUL-2017, entry version 8.
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   ECO:0000313|EMBL:ABJ15162.1};
GN   OrderedLocusNames=PA14_02610 {ECO:0000313|EMBL:ABJ15162.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15162.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15162.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15162.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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: 2'-(5-triphosphoribosyl)-3'-dephospho-CoA +
CC       malonate decarboxylase apo-[acyl-carrier protein] = malonate
CC       decarboxylase holo-[acyl-carrier protein] + diphosphate.
CC       {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; CP000438; ABJ15162.1; -; Genomic_DNA.
DR   RefSeq; WP_003137096.1; NC_008463.1.
DR   EnsemblBacteria; ABJ15162; ABJ15162; PA14_02610.
DR   KEGG; pau:PA14_02610; -.
DR   KO; K13934; -.
DR   OMA; RPHDLLW; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-HAMAP.
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; A0A0H2ZK12.
DR   SWISS-2DPAGE; A0A0H2ZK12.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00650};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00650}.
FT   ACT_SITE    155    155       {ECO:0000256|HAMAP-Rule:MF_00650}.
FT   ACT_SITE    157    157       {ECO:0000256|HAMAP-Rule:MF_00650}.
SQ   SEQUENCE   230 AA;  25286 MW;  68EB239578E50E32 CRC64;
     MVIANSSQRG SSRRRLAPDP MRRRAGPEPH DLLLGMAPAH LPENAPAWVC AALKAGWPVV
     VRRAPADPAR VAIGVRGLVR EQRWAGWMPL AAITWRLRPE ALGQREPAML RDLPAWRALR
     DLRAPLNALG LAWGVTGGAG FELASGVAVL HPDSDLDLLL RTPRPFPRDD ALRLLQRFEQ
     CPCRIDLQLQ TPAGGVALRE WAEGRPRVLA KGSEAPLLLE DPWRVAEVEA
//

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