ID   HCRC_THAAR              Reviewed;         161 AA.
AC   O33818;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   05-MAY-2009, entry version 63.
DE   RecName: Full=4-hydroxybenzoyl-CoA reductase subunit gamma;
DE            EC=1.3.99.20;
GN   Name=hcrC;
OS   Thauera aromatica.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Thauera.
OX   NCBI_TaxID=59405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-19.
RC   STRAIN=DSM 6984 / K172;
RX   MEDLINE=98149712; PubMed=9490068;
RX   DOI=10.1046/j.1432-1327.1998.2510916.x;
RA   Breese K., Fuchs G.;
RT   "4-hydroxybenzoyl-CoA reductase (dehydroxylating) from the
RT   denitrifying bacterium Thauera aromatica -- prosthetic groups,
RT   electron donor, and genes of a member of the molybdenum-flavin-iron-
RT   sulfur proteins.";
RL   Eur. J. Biochem. 251:916-923(1998).
CC   -!- FUNCTION: Catalyzes reductive dehydroxylation of 4-hydroxybenzoyl-
CC       CoA. Reaction is not reversible.
CC   -!- CATALYTIC ACTIVITY: Benzoyl-CoA + acceptor = 4-hydroxybenzoyl-CoA
CC       + reduced acceptor.
CC   -!- COFACTOR: Binds 2 2Fe-2S clusters.
CC   -!- COFACTOR: FAD.
CC   -!- COFACTOR: Molybdenum.
CC   -!- ENZYME REGULATION: Inactivated by low concentrations of cyanide.
CC   -!- SUBUNIT: Heterohexamer of two alpha, two beta and two gamma
CC       subunits.
CC   -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
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DR   EMBL; AJ001830; CAA05037.1; -; Genomic_DNA.
DR   PDB; 1RM6; X-ray; 1.60 A; C/F=1-161.
DR   PDB; 1SB3; X-ray; 2.20 A; C/F=1-161.
DR   PDBsum; 1RM6; -.
DR   PDBsum; 1SB3; -.
DR   BRENDA; 1.3.99.20; 377.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0018525; F:4-hydroxybenzoyl-CoA reductase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002888; 2Fe-2S_bd.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR017606; 4hydrxbenzoyl-CoA_Rdtase_gsu.
DR   InterPro; IPR001041; Ferredoxin.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   ProDom; PD186071; 2Fe-2S_bind; 1.
DR   TIGRFAMs; TIGR03193; 4hydroxCoAred; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3D-structure; Direct protein sequencing; FAD; Flavoprotein;
KW   Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase.
FT   CHAIN         1    161       4-hydroxybenzoyl-CoA reductase subunit
FT                                gamma.
FT                                /FTId=PRO_0000083927.
FT   DOMAIN        3     79       2Fe-2S ferredoxin-type.
FT   METAL        41     41       Iron-sulfur (2Fe-2S) (Potential).
FT   METAL        46     46       Iron-sulfur (2Fe-2S) (Potential).
FT   METAL        49     49       Iron-sulfur (2Fe-2S) (Potential).
FT   METAL        61     61       Iron-sulfur (2Fe-2S) (Potential).
FT   METAL       100    100       Iron-sulfur (2Fe-2S) (Potential).
FT   METAL       103    103       Iron-sulfur (2Fe-2S) (Potential).
FT   METAL       135    135       Iron-sulfur (2Fe-2S) (Potential).
FT   METAL       137    137       Iron-sulfur (2Fe-2S) (Potential).
FT   STRAND        2      9
FT   STRAND       12     19
FT   HELIX        24     30
FT   STRAND       41     46
FT   STRAND       50     53
FT   STRAND       56     59
FT   HELIX        60     62
FT   HELIX        65     68
FT   STRAND       71     74
FT   HELIX        76     78
FT   STRAND       79     81
FT   HELIX        87     94
FT   HELIX       104    117
FT   HELIX       123    129
FT   TURN        130    132
FT   STRAND      136    138
FT   HELIX       141    155
SQ   SEQUENCE   161 AA;  17158 MW;  CC2D8172F8EBA03B CRC64;
     MKNILRLTLN GRAREDLVPD NMLLLDYLRE TVGLTGTKQG CDGGECGACT VLVDDRPRLA
     CSTLAHQVAG KKVETVESLA TQGTLSKLQA AFHEKLGTQC GFCTPGMIMA SEALLRKNPS
     PSRDEIKAAL AGNLCRCTGY VRSSKSVETA AAARLCEEGA R
//