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Database: UniProt
Entry: B5B1B3_9BACT
LinkDB: B5B1B3_9BACT
Original site: B5B1B3_9BACT 
ID   B5B1B3_9BACT            Unreviewed;       267 AA.
AC   B5B1B3;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=3-isopropylcatechol-2,3-dioxygenase-like protein {ECO:0000313|EMBL:ACG59189.1};
DE   Flags: Fragment;
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:ACG59189.1};
RN   [1] {ECO:0000313|EMBL:ACG59189.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19575758; DOI=10.1111/j.1462-2920.2009.01943.x;
RA   Brennerova M.V., Josefiova J., Brenner V., Pieper D.H., Junca H.;
RT   "Metagenomics reveals diversity and abundance of meta-cleavage pathways in
RT   microbial communities from soil highly contaminated with jet fuel under
RT   air-sparging bioremediation.";
RL   Environ. Microbiol. 11:2216-2227(2009).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954,
CC         ECO:0000256|RuleBase:RU000683};
CC   -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC       {ECO:0000256|ARBA:ARBA00008784, ECO:0000256|RuleBase:RU000683}.
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DR   EMBL; EU884894; ACG59189.1; -; Genomic_DNA.
DR   EMBL; EU884897; ACG59192.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5B1B3; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07237; BphC1-RGP6_C_like; 1.
DR   CDD; cd07252; BphC1-RGP6_N_like; 1.
DR   Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 2.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR037523; VOC.
DR   InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2.
DR   PANTHER; PTHR21366; GLYOXALASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR21366:SF34; IRON-DEPENDENT EXTRADIOL DIOXYGENASE; 1.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 2.
DR   PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
DR   PROSITE; PS51819; VOC; 2.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797,
KW   ECO:0000256|RuleBase:RU000683};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU000683};
KW   Iron {ECO:0000256|RuleBase:RU000683};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000683}.
FT   DOMAIN          1..91
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   DOMAIN          115..255
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACG59189.1"
FT   NON_TER         267
FT                   /evidence="ECO:0000313|EMBL:ACG59189.1"
SQ   SEQUENCE   267 AA;  29501 MW;  FE9C53D583E21B93 CRC64;
     LMEVAGSDES AQYRMDSRSW RIAVQKGESD DLAFAGYEVA NPAALQEMTE RLRNAGIQVE
     TGNAELAKRR GVMELISFQD PFGMPLEIYY GATDVFERPF VSSAGVTGFV TGEQGAGHYF
     YVVPSLDEGL AFYTGVLGFQ MSDVIDIAMG PDLTVRGYFL HCNGRHHTLA IAAAPLPKRI
     HHFMLQALTL DDVGHACDRL DGMDDKTIDS NLRLPTKVDR TASCLTTTIG RHVNDHMLSF
     YCATPSGFEL EFGWGAREVD DRSWVMT
//
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