(data stored in ACNUC7421 zone)

SWISSPROT: A0A0H2ZJP0_PSEAB

ID   A0A0H2ZJP0_PSEAB        Unreviewed;       496 AA.
AC   A0A0H2ZJP0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   05-JUL-2017, entry version 14.
DE   RecName: Full=UbiD-like decarboxylase {ECO:0000256|HAMAP-Rule:MF_01983};
DE            EC=4.1.1.- {ECO:0000256|HAMAP-Rule:MF_01983};
DE   AltName: Full=Ferulic acid decarboxylase-like protein {ECO:0000256|HAMAP-Rule:MF_01983};
GN   OrderedLocusNames=PA14_03130 {ECO:0000313|EMBL:ABJ15203.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15203.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15203.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15203.1,
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: Catalyzes the reversible decarboxylation of aromatic
CC       carboxylic acids. {ECO:0000256|HAMAP-Rule:MF_01983}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01983};
CC       Name=prenyl-FMN; Xref=ChEBI:CHEBI:87746;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01983};
CC       Note=Binds 1 prenylated FMN (prenyl-FMN) per subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_01983};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01983}.
CC   -!- SIMILARITY: Belongs to the UbiD family. UbiD-like/FDC subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01983}.
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DR   EMBL; CP000438; ABJ15203.1; -; Genomic_DNA.
DR   RefSeq; WP_003137133.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZJP0; -.
DR   EnsemblBacteria; ABJ15203; ABJ15203; PA14_03130.
DR   KEGG; pau:PA14_03130; -.
DR   KO; K03182; -.
DR   OMA; THFHAYV; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01983; UbiD_FDC; 1.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   InterPro; IPR002830; UbiD.
DR   InterPro; IPR032903; UbiD/Fdc1.
DR   Pfam; PF01977; UbiD; 1.
DR   SUPFAM; SSF50475; SSF50475; 1.
DR   TIGRFAMs; TIGR00148; TIGR00148; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZJP0.
DR   SWISS-2DPAGE; A0A0H2ZJP0.
KW   Aromatic hydrocarbons catabolism {ECO:0000256|HAMAP-Rule:MF_01983};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_01983};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01983};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01983};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01983}.
FT   REGION      165    170       prenyl-FMN binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01983}.
FT   REGION      187    188       prenyl-FMN binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01983}.
FT   ACT_SITE    278    278       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01983}.
FT   METAL       188    188       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_01983}.
FT   METAL       229    229       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_01983}.
SQ   SEQUENCE   496 AA;  54443 MW;  772C9C6F83DB72E5 CRC64;
     MNRSALDFRH FIDHLRRQGD LVDVHTEVDA NLEIGAITRR VYERRAPAPL FHNIRDSLPG
     ARVLGAPAGL RADRARAHSR LALHFGLPEH SGPRDIVATL RAAMRAEPIA PRRLERGPVQ
     ENVWLGEQVD LTRFPVPLLH EQDGGRYFGT YGFHVVQTPD GSWDSWSVGR LMLVDRNTLA
     GPTIPTQHIG IIREQWRRQG KPTPWAMALG APPAALAAAG MPLPEGVSEA GYVGALVGEP
     VEVVRTQTNG LWVPANAEIV LEGEISLDET ALEGPMGEYH GYSFPTGKPQ PLFHVHALSF
     RDQPILPICV AGTPPEENHT IWGTMISAQL LDVAQNAGLP VDMAWCSYEA ATCWAVLSID
     VQRLAALGTD AAAFAARVAE TVFGSHAGHL VPKLILVGND IDVTEIDQVV WALATRAHPL
     HDHFAFPQIR DFPMVPYLDA EDKARGSGGR LVINCLYPEQ FAGQMRAATA SFRHAYPTAL
     RRRVEERWSD YGFADA
//

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