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Database: UniProt
Entry: S3UUM9_9LEPT
LinkDB: S3UUM9_9LEPT
Original site: S3UUM9_9LEPT 
ID   S3UUM9_9LEPT            Unreviewed;       298 AA.
AC   S3UUM9;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Aromatic ring-opening dioxygenase, catalytic subunit LigB {ECO:0000313|EMBL:EPG72953.1};
GN   ORFNames=LEP1GSC058_2438 {ECO:0000313|EMBL:EPG72953.1};
OS   Leptospira fainei serovar Hurstbridge str. BUT 6.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1193011 {ECO:0000313|EMBL:EPG72953.1, ECO:0000313|Proteomes:UP000014540};
RN   [1] {ECO:0000313|EMBL:EPG72953.1, ECO:0000313|Proteomes:UP000014540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BUT 6 {ECO:0000313|EMBL:EPG72953.1,
RC   ECO:0000313|Proteomes:UP000014540};
RA   Harkins D.M., Durkin A.S., Selengut J.D., Sanka R., DePew J., Purushe J.,
RA   Ahmed A., van der Linden H., Goris M.G.A., Hartskeerl R.A., Vinetz J.M.,
RA   Sutton G.G., Nelson W.C., Fouts D.E.;
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPG72953.1}.
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DR   EMBL; AKWZ02000010; EPG72953.1; -; Genomic_DNA.
DR   AlphaFoldDB; S3UUM9; -.
DR   STRING; 1193011.LEP1GSC058_2438; -.
DR   OrthoDB; 9790889at2; -.
DR   Proteomes; UP000014540; 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:EPG72953.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          65..278
FT                   /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT                   subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF02900"
SQ   SEQUENCE   298 AA;  33275 MW;  A6304AD60C1BB4AB CRC64;
     MDQIGSDGEK FSRRKFLGGA LASFLVALGV GKRFSGKKGD SEMNRAPVFF VGHGSPMNAI
     GENEFTKGWA ASVQNLPRPK AILCISAHWV TRGSRITAME SPKTIHDFYG FPQELFDVQY
     SAPGNPALAK EISTDSRTQR LDLDYEWGLD HGSWSVLRHM YPNADIPVLQ LSLDATKPAG
     WHYEFAKELA SLRDQNTLIV GSGDLVHNLR LYNWRNEEEI PDWSKEANET FKALILKRDS
     KALSQYQNLG TAAQLAVPTP EHYIPMLYAL ALAGENEEIS FYNDKIQSTV SMTSFRIG
//
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