ID G8NV36_GRAMM Unreviewed; 325 AA.
AC G8NV36;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Glyoxalase/bleomycin resistance protein/dioxygenase {ECO:0000313|EMBL:AEU38806.1};
DE Flags: Precursor;
GN OrderedLocusNames=AciX8_4535 {ECO:0000313|EMBL:AEU38806.1};
OS Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU38806.1, ECO:0000313|Proteomes:UP000007113};
RN [1] {ECO:0000313|EMBL:AEU38806.1, ECO:0000313|Proteomes:UP000007113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8
RC {ECO:0000313|Proteomes:UP000007113};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M.,
RA Haggblom M., Woyke T.;
RT "Complete sequence of Granulicella mallensis MP5ACTX8.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003130; AEU38806.1; -; Genomic_DNA.
DR RefSeq; WP_014267677.1; NC_016631.1.
DR AlphaFoldDB; G8NV36; -.
DR STRING; 682795.AciX8_4535; -.
DR KEGG; gma:AciX8_4535; -.
DR eggNOG; COG0346; Bacteria.
DR HOGENOM; CLU_952371_0_0_0; -.
DR OrthoDB; 108351at2; -.
DR Proteomes; UP000007113; Chromosome.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR CDD; cd06587; VOC; 2.
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 PANTHER; PTHR43048; METHYLMALONYL-COA EPIMERASE; 1.
DR PANTHER; PTHR43048:SF3; METHYLMALONYL-COA EPIMERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00903; Glyoxalase; 2.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 2.
DR PROSITE; PS51819; VOC; 2.
PE 4: Predicted;
KW Dioxygenase {ECO:0000313|EMBL:AEU38806.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:AEU38806.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007113};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..325
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003512941"
FT DOMAIN 39..158
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 180..304
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT REGION 304..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 325 AA; 36244 MW; F39E3E53BA4C04D0 CRC64;
MNLRRIFNPS RYAVLLGVLS LTLCANAQST APQRPRITGI SHVGYFVSNL QASIAFWHDF
LGFDEAYDLK KPGSDETRIA FIKINDHQHI ELFNEVPSDT RNMMSHICFT VDDVEQMRTY
LKSQGLNVKP GNGSKTRTGD YAFEIKDPDG TLVEFVQSLP DGLEKKAAGK FLPDTRISTK
IYHAGFLVGN SQRSLDFYGK VLGFKETWRG GGNPAELSWI NMRVPDGDDY VEFMLYRKLP
TDSWGGKNHL SLEVPDVTKA VETLEARPAF KTYGKPLTVA TGINHKHQVN IFDPDGTRVE
LMESHTIDGK PVSSSTAPPP PPSHD
//
