ID   U4QQL0_9BACT            Unreviewed;       291 AA.
AC   U4QQL0;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Putative catalytic LigB subunit of aromatic ring-opening dioxygenase {ECO:0000313|EMBL:EIJ75984.1};
GN   ORFNames=C75L2_00080001 {ECO:0000313|EMBL:EIJ75984.1};
OS   Leptospirillum sp. Group II 'C75'.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=1159328 {ECO:0000313|EMBL:EIJ75984.1, ECO:0000313|Proteomes:UP000016760};
RN   [1] {ECO:0000313|EMBL:EIJ75984.1, ECO:0000313|Proteomes:UP000016760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22539719; DOI=10.1126/science.1218389;
RA   Denef V.J., Banfield J.F.;
RT   "In situ evolutionary rate measurements show ecological success of recently
RT   emerged bacterial hybrids.";
RL   Science 336:462-466(2012).
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; JH660592; EIJ75984.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4QQL0; -.
DR   HOGENOM; CLU_046582_2_1_0; -.
DR   Proteomes; UP000016760; Unassembled WGS sequence.
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:EIJ75984.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          11..237
FT                   /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT                   subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF02900"
FT   REGION          265..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   291 AA;  32222 MW;  687E9AB441F38E58 CRC64;
     MATFERFSAV FLSHGAPNIL LEDSPASRFL KRLGSLIEKP ERILVVSAHW QTVLPTIGAS
     SVFETLHDFY GFEEALYRVR YPARGVPEEA RRLQENLKNL GIPCLIETQR GLDHGAWVPL
     MALYPAADVP VIPVSLPQSF SPDDLIQLGT FLRESFPEKT LLIGSGGITH NLFAYRPGRP
     PYPQVVAFDA WLKDNLLKKN TGALLDFQSG APETRFNHPT EEHLLPLFVV MGFGYDTPCP
     VLLHEEISGG SLSLASYGFP RPGQAEVPDW ESLESDPKPS SWNTGSLPLS E
//