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Database: UniProt
Entry: W5WF48_9PSEU
LinkDB: W5WF48_9PSEU
Original site: W5WF48_9PSEU 
ID   W5WF48_9PSEU            Unreviewed;       345 AA.
AC   W5WF48;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=VOC domain-containing protein {ECO:0000259|PROSITE:PS51819};
GN   ORFNames=KALB_6025 {ECO:0000313|EMBL:AHH99385.1};
OS   Kutzneria albida DSM 43870.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Kutzneria.
OX   NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH99385.1, ECO:0000313|Proteomes:UP000019225};
RN   [1] {ECO:0000313|EMBL:AHH99385.1, ECO:0000313|Proteomes:UP000019225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH99385.1};
RX   PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA   Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA   Bechthold A., Kalinowski J., Luzhetskyy A.;
RT   "Complete genome sequence of producer of the glycopeptide antibiotic
RT   Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT   of Pseudonocardiaceae.";
RL   BMC Genomics 15:885-885(2014).
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; CP007155; AHH99385.1; -; Genomic_DNA.
DR   AlphaFoldDB; W5WF48; -.
DR   STRING; 1449976.KALB_6025; -.
DR   KEGG; kal:KALB_6025; -.
DR   PATRIC; fig|1449976.3.peg.6047; -.
DR   eggNOG; COG0346; Bacteria.
DR   HOGENOM; CLU_052361_3_0_11; -.
DR   OrthoDB; 317332at2; -.
DR   Proteomes; UP000019225; 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; cd07256; HPCD_C_class_II; 1.
DR   Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 2.
DR   Gene3D; 4.10.1270.10; homoprotocatechuate 2,3-dioxygenase domains; 1.
DR   InterPro; IPR011981; DHPA_dOase_Mn/Fe.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR044904; HPCD_C_sf.
DR   InterPro; IPR037523; VOC.
DR   InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2.
DR   NCBIfam; TIGR02295; HpaD; 1.
DR   PANTHER; PTHR21366:SF27; BLL2967 PROTEIN; 1.
DR   PANTHER; PTHR21366; GLYOXALASE FAMILY PROTEIN; 1.
DR   Pfam; PF00903; Glyoxalase; 2.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019225}.
FT   DOMAIN          9..123
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   DOMAIN          144..263
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
SQ   SEQUENCE   345 AA;  39032 MW;  D205588004B18EC0 CRC64;
     MSTAPDVIRC AYAEFVVSDL RASRAFYVDV LGLVVTHEDA DTIHLRAFEE YLHHSLVLRR
     GPVPALAVLG YRVRTPADLD LAEAYYRELG VRVRRREPGA TLGIGEAVRV EDPLGFPIEF
     FHEAVHVERF TQRYDTHGAG AISRLDHFNL NTPDVPAARK YYEGLGFRVS EDIQDSDGTV
     YAAWMFRKPT VHDVALTGGD GPRLHHIAFA THERHQILHI CDHLGALRQS DMIERGPGRH
     GVSNAFYLYL RDPDGHRIEI YTHDYYTGDP DNPVITWDVH DNQRRDWWGN AVVPSWYTEA
     SPVLDLDGAP RPLVARTDAR EMDVTIGADG FSYTRSTEFK LGEQV
//
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