ID A0A1V6U841_9EURO Unreviewed; 485 AA.
AC A0A1V6U841;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=PENCOP_c016G04443 {ECO:0000313|EMBL:OQE34658.1};
OS Penicillium coprophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE34658.1, ECO:0000313|Proteomes:UP000191500};
RN [1] {ECO:0000313|Proteomes:UP000191500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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:OQE34658.1}.
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DR EMBL; MDDG01000016; OQE34658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6U841; -.
DR STRING; 36646.A0A1V6U841; -.
DR OrthoDB; 38879at2759; -.
DR Proteomes; UP000191500; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR045054; P4HA-like.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR PANTHER; PTHR10869:SF207; P4HA_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000191500}.
FT DOMAIN 355..477
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 52866 MW; A6D0EF6F43891F9A CRC64;
MAKSKAAKRK RNAQVDLPQK LPKAVPNLTP PPDGGTPEST HVNAVVSDEE LDITIETLAA
LAQYPSVTKS KACKDLRVAV YDFRQACTTG VNTAEGANLT ARITGALADE KYIEARILLA
EMRIRKEQPK IGALCRWVRD LDVVSGLSTQ PKAHDNAPVK RSAKEMEILG VLDAILRVST
PIDTNTNAVD STAPIAFQSI WDLRPSTAPL PVYASVLDKS ILSEAPRSPS ALRVIERTPG
PLRKPPNHHP AILYTTAPNA VPLAPVGPPI TYHAHPAVPG LGLALNVLSD AECKAIIAAG
ESVNFLPDAP LREDGDISIL AHNFYWIIDT TFHDMLWARV SPYVPPSIGG RLVRGINRRF
RVYRYVPGAE YRCHIDGAWP PSGILPDDTY VYDSSPEDKK QSSMYTFLLY LNDEFEGGET
TFFMPAPREG TLNGYPVRPV MGAVAIFPHG ESNGALLHEG TGVRKGAKYI IRTDVEYDVK
PCEEG
//
