ID B0JEB6_9BACT Unreviewed; 149 AA.
AC B0JEB6;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Aromatic ring-hydroxylating dioxygenase {ECO:0000313|EMBL:CAP60634.1};
DE Flags: Fragment;
GN Name=arhd {ECO:0000313|EMBL:CAP60634.1};
GN Synonyms=ARHD {ECO:0000313|EMBL:ADD71869.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:CAP60634.1};
RN [1] {ECO:0000313|EMBL:CAP60634.1}
RP NUCLEOTIDE SEQUENCE.
RA Lozada M., Riva Mercadal J.P., Guerrero L.D., Di Marzio W.D., Ferrero M.A.,
RA Dionisi H.M.;
RT "Novel aromatic ring-hydroxylating dioxygenase genes from coastal marine
RT sediments of Patagonia .";
RL BMC Microbiol. 8:50-50(2008).
RN [2] {ECO:0000313|EMBL:ADD71869.1}
RP NUCLEOTIDE SEQUENCE.
RA Dionisi H.M., Lozada M., Marcos M.S., Di Marzio W.D., Loviso C.L.;
RT "Aromatic hydrocarbon degradation genes from chronically polluted
RT Subantarctic marine sediments.";
RL (In) de Bruijn F.J. (eds.);
RL HANDBOOK OF MOLECULAR MICROBIAL ECOLOGY II: METAGENOMICS IN DIFFERENT
RL HABITATS, pp.0-0, Wiley-Blackwell, 111 River Street, Hoboken, NJ, USA
RL (2010).
RN [3] {ECO:0000313|EMBL:ADD71869.1}
RP NUCLEOTIDE SEQUENCE.
RA Loviso C.L., Lozada M., Dionisi H.M.;
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR EMBL; GU563541; ADD71869.1; -; Genomic_DNA.
DR EMBL; AM930935; CAP60634.1; -; Genomic_DNA.
DR AlphaFoldDB; B0JEB6; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756:SF1; 3-PHENYLPROPIONATE_CINNAMIC ACID DIOXYGENASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43756; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR Pfam; PF00355; Rieske; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Dioxygenase {ECO:0000313|EMBL:CAP60634.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..77
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAP60634.1"
FT NON_TER 149
FT /evidence="ECO:0000313|EMBL:CAP60634.1"
SQ SEQUENCE 149 AA; 16209 MW; 9B976B9B1EE32D66 CRC64;
ESAIPDAGDF FTTFMGQDAV LVVRQDDGSV KAFLNYCQHR GNKVCFADSG NAKAFTCNYH
GWSYGGDGRL AAVPLEHEVY LGGFDRAAHA LEPIAQVASY RGFVFGCMDP DAPPLAEYLG
EMGWYLDSFM VGDGQGAELV RPPMKSILR
//
