ID A1T2N0_MYCVP Unreviewed; 327 AA.
AC A1T2N0;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Glyoxalase/bleomycin resistance protein/dioxygenase {ECO:0000313|EMBL:ABM11430.1};
GN OrderedLocusNames=Mvan_0591 {ECO:0000313|EMBL:ABM11430.1};
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM11430.1, ECO:0000313|Proteomes:UP000009159};
RN [1] {ECO:0000313|EMBL:ABM11430.1, ECO:0000313|Proteomes:UP000009159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1 {ECO:0000313|Proteomes:UP000009159};
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 Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000511; ABM11430.1; -; Genomic_DNA.
DR RefSeq; WP_011777867.1; NZ_JACKSD010000118.1.
DR AlphaFoldDB; A1T2N0; -.
DR STRING; 350058.Mvan_0591; -.
DR KEGG; mva:Mvan_0591; -.
DR eggNOG; COG0346; Bacteria.
DR HOGENOM; CLU_052361_2_0_11; -.
DR Proteomes; UP000009159; Chromosome.
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; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000009159}.
FT DOMAIN 10..124
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 146..273
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
SQ SEQUENCE 327 AA; 36684 MW; 3A999C8B9A77C5C4 CRC64;
MTPDVFGKVH LGYLVIESDR FADWRRFGRD AIGMHLDETL TDVMRFRLDD NACRFLLTRG
PAEDTTALGW EVGDHDTFDA IAARIHDHGV PVSDGAAEEA EIRGVEHFIR FPGPNGLLQE
LYVTPRKGLQ HLRLGVAGGF VTGVDGMGHV AIATKKPHQM HGYYRTVFDA RLSDYIDETI
SGLKFKIRFL RVNERHHSVA IASVNRLPLN PIRTRIQHCN IQVAELDDMA SAYRRVKELG
FEMALSVGQH TNDKELSFYA VTPSGFEWEV GWNPIVVDEA TWEPTTHQGI SLWGHTPEGH
TIVNLLERFK AGARSVFHAE DSVPALV
//
