(data stored in ACNUC7421 zone)

SWISSPROT: A0A0H2ZJE9_PSEAB

ID   A0A0H2ZJE9_PSEAB        Unreviewed;       310 AA.
AC   A0A0H2ZJE9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 10.
DE   RecName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000256|PIRNR:PIRNR000446};
DE            EC=2.3.1.39 {ECO:0000256|PIRNR:PIRNR000446};
GN   Name=mdcH {ECO:0000313|EMBL:ABJ15163.1};
GN   OrderedLocusNames=PA14_02620 {ECO:0000313|EMBL:ABJ15163.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15163.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15163.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15163.1,
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   -!- CATALYTIC ACTIVITY: Malonyl-CoA + an [acyl-carrier-protein] = CoA
CC       + a malonyl-[acyl-carrier-protein].
CC       {ECO:0000256|PIRNR:PIRNR000446}.
CC   -!- SIMILARITY: Belongs to the fabD family.
CC       {ECO:0000256|PIRNR:PIRNR000446}.
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DR   EMBL; CP000438; ABJ15163.1; -; Genomic_DNA.
DR   RefSeq; WP_003137098.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZJE9; -.
DR   EnsemblBacteria; ABJ15163; ABJ15163; PA14_02620.
DR   KEGG; pau:PA14_02620; -.
DR   KO; K13935; -.
DR   OMA; NINADNQ; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR017554; Malonate_deCOase_MdcHsu.
DR   InterPro; IPR024925; Malonyl_CoA-ACP_transAc.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR020801; PKS_acyl_transferase.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   PIRSF; PIRSF000446; Mct; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; SSF52151; 2.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   TIGRFAMs; TIGR03131; malonate_mdcH; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZJE9.
DR   SWISS-2DPAGE; A0A0H2ZJE9.
KW   Acyltransferase {ECO:0000256|PIRNR:PIRNR000446};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000446}.
FT   DOMAIN        6    305       PKS_AT. {ECO:0000259|SMART:SM00827}.
FT   ACT_SITE     86     86       {ECO:0000256|PIRSR:PIRSR000446-1}.
FT   ACT_SITE    195    195       {ECO:0000256|PIRSR:PIRSR000446-1}.
SQ   SEQUENCE   310 AA;  32739 MW;  F38EF3358300922C CRC64;
     MSVLFAYPGQ GAQRPGMLAA LPDEPPVRAC LEQAADCLGQ APAELESAEA LRGTRAVQLC
     LLIAGVAASR LLETRGHRPG LVAGLSIGAY PAAVVAGALD FDDALRLVAL RGELMQAAWP
     EGYGMSAILG LDQAQLDALI LMVRREHPPL YLANVNAERQ LVVAGSEAAL AALAERARAA
     GASAAKRLAV SVPSHCALLD EPAARLAEAF AGVRLRRPRV PYLSSSRARL VAEPAALADD
     LAGNMARRVE WLATLRSAYE RGARLHLELP PGRVLSGLAR PLFGCATPAF EGSRADTLDA
     LLREEEKRTR
//

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