(data stored in ACNUC9435 zone)

SWISSPROT: HPDA_CLOD6

ID   HPDA_CLOD6              Reviewed;         316 AA.
AC   Q18CP3;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   11-DEC-2019, entry version 80.
DE   RecName: Full=4-hydroxyphenylacetate decarboxylase activating enzyme {ECO:0000250|UniProtKB:Q84F14};
DE            Short=Hpd-AE {ECO:0000250|UniProtKB:Q84F14};
DE            EC=1.97.1.-;
GN   Name=hpdA {ECO:0000312|EMBL:CAJ66975.1}; OrderedLocusNames=CD630_01550;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
CC   -!- FUNCTION: Activation of 4-hydroxyphenylacetate decarboxylase under
CC       anaerobic conditions by generation of an organic free radical.
CC       {ECO:0000250|UniProtKB:Q46267, ECO:0000250|UniProtKB:Q84F14}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q84F14};
CC       Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250|UniProtKB:Q84F14};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q84F14}.
CC   -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC       {ECO:0000255}.
DR   EMBL; AM180355; CAJ66975.1; -; Genomic_DNA.
DR   RefSeq; WP_011860651.1; NZ_CP010905.2.
DR   RefSeq; YP_001086624.1; NC_009089.1.
DR   STRING; 272563.CD630_01550; -.
DR   DNASU; 4914361; -.
DR   EnsemblBacteria; CAJ66975; CAJ66975; CD630_01550.
DR   GeneID; 4914361; -.
DR   KEGG; cdf:CD630_01550; -.
DR   KEGG; pdc:CDIF630_00274; -.
DR   PATRIC; fig|272563.120.peg.168; -.
DR   eggNOG; ENOG4105F1A; Bacteria.
DR   eggNOG; COG1180; LUCA.
DR   HOGENOM; HOG000011459; -.
DR   OMA; HTLGMNK; -.
DR   Proteomes; UP000001978; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 2.
DR   InterPro; IPR034438; 4-hPhe_decarboxylase_activase.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR040074; BssD/PflA/YjjW.
DR   InterPro; IPR034457; Organic_radical-activating.
DR   InterPro; IPR012839; Organic_radical_activase.
DR   InterPro; IPR001989; Radical_activat_CS.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR30352; PTHR30352; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF000371; PFL_act_enz; 1.
DR   SFLD; SFLDF00279; 4-hydroxyphenylacetate_decarbo; 1.
DR   SFLD; SFLDG01118; activating_enzymes__group_2; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS01087; RADICAL_ACTIVATING; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q18CP3.
DR   SWISS-2DPAGE; Q18CP3.
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW   Reference proteome; S-adenosyl-L-methionine.
FT   CHAIN           1..316
FT                   /note="4-hydroxyphenylacetate decarboxylase activating
FT                   enzyme"
FT                   /id="PRO_0000403683"
FT   DOMAIN          84..115
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   REGION          40..42
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   REGION          193..195
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   METAL           34
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   METAL           38
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   METAL           41
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         144
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         267
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen and
FT                   carbonyl oxygen"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
SQ   SEQUENCE   316 AA;  35946 MW;  911B3DB1B8344624 CRC64;
     MSSQKQLEGM IFDVQSFSVH DGPGCRTTVF LNGCPLSCKW CANPESWTVR PHMMFSELSC
     QYENGCTVCH GKCKNGALSF NLDNKPVIDW NICKDCESFE CVNSCYYNAF KLCAKPYTVD
     ELVQVIKRDS NNWRSNGGVT FSGGEPLLQH EFLHEVLLKC HEVNIHTAIE TSACVSNEVF
     NKIFNDIDFA FIDIKHMDRE KHKEQTGVYN DLILENISNL ANSDWNGRLV LRVPVISGFN
     DSDENISDII SFMHKNNLVE INLLPFHRLG ESKWTQLGKE YEYSDKGDVD EGHLEELQDI
     FLDNGIACYV GHETAF
//

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