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Database: UniProt
Entry: B4U9M1_HYDS0
LinkDB: B4U9M1_HYDS0
Original site: B4U9M1_HYDS0 
ID   B4U9M1_HYDS0            Unreviewed;       240 AA.
AC   B4U9M1;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Extradiol ring-cleavage dioxygenase class III protein subunit B {ECO:0000313|EMBL:ACG57832.1};
GN   ORFNames=HY04AAS1_1146 {ECO:0000313|EMBL:ACG57832.1};
OS   Hydrogenobaculum sp. (strain Y04AAS1).
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae;
OC   Hydrogenobaculum.
OX   NCBI_TaxID=380749 {ECO:0000313|EMBL:ACG57832.1};
RN   [1] {ECO:0000313|EMBL:ACG57832.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Y04AAS1 {ECO:0000313|EMBL:ACG57832.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Kiss H., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Resenback A.-L., Mead D.;
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACG57832.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Y04AAS1 {ECO:0000313|EMBL:ACG57832.1};
RX   PubMed=19136599; DOI=10.1128/JB.01645-08;
RA   Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the DODA-type extradiol aromatic ring-opening
CC       dioxygenase family. {ECO:0000256|ARBA:ARBA00007581}.
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DR   EMBL; CP001130; ACG57832.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4U9M1; -.
DR   STRING; 380749.HY04AAS1_1146; -.
DR   KEGG; hya:HY04AAS1_1146; -.
DR   eggNOG; COG3384; Bacteria.
DR   HOGENOM; CLU_046582_2_0_0; -.
DR   OrthoDB; 9790889at2; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0016701; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR   CDD; cd07363; 45_DOPA_Dioxygenase; 1.
DR   Gene3D; 3.40.830.10; LigB-like; 1.
DR   InterPro; IPR014436; Extradiol_dOase_DODA.
DR   InterPro; IPR004183; Xdiol_dOase_suB.
DR   PANTHER; PTHR30096:SF0; 4,5-DOPA DIOXYGENASE EXTRADIOL-LIKE PROTEIN; 1.
DR   PANTHER; PTHR30096; UNCHARACTERIZED; 1.
DR   Pfam; PF02900; LigB; 1.
DR   PIRSF; PIRSF006157; Doxgns_DODA; 1.
DR   SUPFAM; SSF53213; LigB-like; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000313|EMBL:ACG57832.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          2..218
FT                   /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT                   subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF02900"
SQ   SEQUENCE   240 AA;  27806 MW;  51B02AB545C1DFE5 CRC64;
     MIYFISHGSP MLLLENNDFT KMLKNQEKRI KSSKYIIVLS SHWLTEEPMI SENPYPIMYD
     FYGFPKELYS IDYKAFTDKN IVDSISSKLH LAKTKRGLDH GAWALLYHML KDASLPIVQI
     SIPIGKDLDF YIDFGEKLSH FKDEASILFS GGAIHNLMLI KDTTEDWAYE FHDFIKNAVL
     NHDIKSLKNF KHHRYANIAH PTIEHFIPLF YFIGACQRPT LLYDGFELGN LSLLSFGCIN
//
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