ID A1UDF5_MYCSK Unreviewed; 296 AA.
AC A1UDF5;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Glyoxalase/bleomycin resistance protein/dioxygenase {ECO:0000313|EMBL:ABL90863.1};
GN OrderedLocusNames=Mkms_1656 {ECO:0000313|EMBL:ABL90863.1};
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL90863.1};
RN [1] {ECO:0000313|EMBL:ABL90863.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:ABL90863.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000518; ABL90863.1; -; Genomic_DNA.
DR AlphaFoldDB; A1UDF5; -.
DR STRING; 189918.Mkms_1656; -.
DR KEGG; mkm:Mkms_1656; -.
DR HOGENOM; CLU_052361_2_0_11; -.
DR OrthoDB; 6909416at2; -.
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; 1.
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 5..119
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 142..258
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
SQ SEQUENCE 296 AA; 32496 MW; B3AF3EF75B24A7D4 CRC64;
MLVKALGYVG VESPDAKEWL AFGPEVLGME AVEASSGSVL LRIDDADHRL AVHHGERNRM
LYAGWDVGSE EALEAAGELL HKRGIGFEVG TEEDCAARGV LGFVTLSDPS GLRHELFYGQ
KVVPGSFRPG RAMSGFVTGA QGLGHVVLAT PDLAQADRFL RGVLGFKKSD EIYTFMDLWF
YHCNPRHHSI ALTPMPGVRG LHHVMVEVQS FDDVGMAYDL CMSRNIPLSM TLGRHVNDRM
VSFYARTPSG FDIEYGWDAV TVDEETWTVA QYDRPSVWGH QMVAQTPPGA LEAATT
//
