ID A0A0D8HSY5_RHOSX Unreviewed; 320 AA.
AC A0A0D8HSY5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Deacetoxycephalosporin C hydroxylase {ECO:0000313|EMBL:KJF21110.1};
DE EC=1.14.11.26 {ECO:0000313|EMBL:KJF21110.1};
GN Name=cefF_2 {ECO:0000313|EMBL:KJF21110.1};
GN ORFNames=SZ00_04315 {ECO:0000313|EMBL:KJF21110.1};
OS Rhodococcus sp. (strain AD45).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=103808 {ECO:0000313|EMBL:KJF21110.1, ECO:0000313|Proteomes:UP000032323};
RN [1] {ECO:0000313|EMBL:KJF21110.1, ECO:0000313|Proteomes:UP000032323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD45 {ECO:0000313|EMBL:KJF21110.1,
RC ECO:0000313|Proteomes:UP000032323};
RX PubMed=25727256; DOI=10.1111/1462-2920.12793;
RA Crombie A.T., El Khawand M., Rhodius V.A., Fengler K.A., Miller M.C.,
RA Whited G.M., McGenity T.J., Murrell J.C.;
RT "Regulation of plasmid-encoded isoprene metabolism in Rhodococcus, a
RT representative of an important link in the global isoprene cycle.";
RL Environ. Microbiol. 17:3314-3329(2015).
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|RuleBase:RU003682}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJF21110.1}.
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DR EMBL; JYOP01000003; KJF21110.1; -; Genomic_DNA.
DR RefSeq; WP_033234036.1; NZ_JYOP01000003.1.
DR AlphaFoldDB; A0A0D8HSY5; -.
DR PATRIC; fig|103808.5.peg.4828; -.
DR OrthoDB; 21825at2; -.
DR Proteomes; UP000032323; Unassembled WGS sequence.
DR GO; GO:0045442; F:deacetoxycephalosporin-C hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; 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 PRINTS; PR00682; IPNSYNTHASE.
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 ECO:0000313|EMBL:KJF21110.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032323}.
FT DOMAIN 173..283
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 320 AA; 35488 MW; AF7EC3F8DDEFED64 CRC64;
MNTIPLVDLE QWRTGSSLQR AKLSERVDQA LQGSGFLLIS GHGIDPELRA QIRAAGSAFF
TSGPATKHRY RTHVGGRGWI PSGAEANAFV EETPGPADLK ETYTNGWDDY STGDPVVDNE
WFAPNVWPTE VPEFERLCAT YTEQMRSLAA ELLTVFASAL NLDPDWFTSR TDRAPHSFNL
NRYPAMAETG IAIDGQYRIA PHTDFGVITI LDRQAGYGGL QVDTGDGSWV NAPFVDDAFT
INIGDLMARW TGDRWRSTRH RVLPPSAHDP NEELISLIFF FEANHDAVIE SFGPPIGRAH
AYQPVTTADY LRARYSAITI
//
