ID H6MZC3_GORPV Unreviewed; 334 AA.
AC H6MZC3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Putative oxidoreductase, 2OG-Fe(II) oxygenase family {ECO:0000313|EMBL:AFA75665.1};
GN OrderedLocusNames=GPOL_c46650 {ECO:0000313|EMBL:AFA75665.1};
OS Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA75665.1, ECO:0000313|Proteomes:UP000009154};
RN [1] {ECO:0000313|EMBL:AFA75665.1, ECO:0000313|Proteomes:UP000009154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA Liebl W., Daniel R., Steinbuchel A.;
RT "Involvement of two latex-clearing proteins during rubber degradation and
RT insights into the subsequent degradation pathway revealed by the genome
RT sequence of Gordonia polyisoprenivorans strain VH2.";
RL Appl. Environ. Microbiol. 78:2874-2887(2012).
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|RuleBase:RU003682}.
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; CP003119; AFA75665.1; -; Genomic_DNA.
DR RefSeq; WP_014361823.1; NC_016906.1.
DR AlphaFoldDB; H6MZC3; -.
DR STRING; 1112204.GPOL_c46650; -.
DR KEGG; gpo:GPOL_c46650; -.
DR eggNOG; COG3491; Bacteria.
DR HOGENOM; CLU_010119_6_2_11; -.
DR Proteomes; UP000009154; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR47990:SF258; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Iron {ECO:0000256|RuleBase:RU003682};
KW Metal-binding {ECO:0000256|RuleBase:RU003682};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW Reference proteome {ECO:0000313|Proteomes:UP000009154}.
FT DOMAIN 186..296
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 334 AA; 35841 MW; D2615FBB956D43A3 CRC64;
MTAANPRTAN PQTASPILTV DLQQWRQGGD AAAQVCAAVD ESLQKAGFLL VTGHGIDPFL
PAALRAAARE FFALPAEVKA QYAVGVGGRG WIGPGLEANG YAEGTETPPD LKETYNSGAQ
TPVGIPEVDD YWFAPDVWPA ETPRLRELFT AWTSQMKALS DDLLALMAEA LGKAGEDNPF
RNLAGNATWT SNINHYPPMT VVGDPEPGQF RIGPHTDFGT VTVLDREPGA GGLQVYSDES
GWADAPYDPT ALTINIGDLL EYWSGGRWPA GRHRVLPPQP ESPEEDLVSL IFFYELDHDA
VVTPLAPPVG RVSGRPDVIA GEFIKERLDA ITLG
//