ID A0A094CEL1_9PEZI Unreviewed; 710 AA.
AC A0A094CEL1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Extradiol ring-cleavage dioxygenase class III enzyme subunit B domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=V491_03230 {ECO:0000313|EMBL:KFY21022.1};
OS Pseudogymnoascus sp. VKM F-3775.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420901 {ECO:0000313|EMBL:KFY21022.1, ECO:0000313|Proteomes:UP000029338};
RN [1] {ECO:0000313|EMBL:KFY21022.1, ECO:0000313|Proteomes:UP000029338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3775 {ECO:0000313|EMBL:KFY21022.1,
RC ECO:0000313|Proteomes:UP000029338};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the DODA-type extradiol aromatic ring-opening
CC dioxygenase family. {ECO:0000256|ARBA:ARBA00007581}.
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:KFY21022.1}.
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DR EMBL; JPJT01001855; KFY21022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094CEL1; -.
DR HOGENOM; CLU_388889_0_0_1; -.
DR Proteomes; UP000029338; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProt.
DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016701; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR CDD; cd07363; 45_DOPA_Dioxygenase; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1.
DR Gene3D; 3.40.830.10; LigB-like; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR016170; Cytok_DH_C_sf.
DR InterPro; IPR014436; Extradiol_dOase_DODA.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR InterPro; IPR004183; Xdiol_dOase_suB.
DR PANTHER; PTHR30096:SF0; 4,5-DOPA DIOXYGENASE EXTRADIOL-LIKE PROTEIN; 1.
DR PANTHER; PTHR30096; UNCHARACTERIZED; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF02900; LigB; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR SUPFAM; SSF53213; LigB-like; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000029338};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 10..254
FT /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT subunit B"
FT /evidence="ECO:0000259|Pfam:PF02900"
FT DOMAIN 319..447
FT /note="FAD linked oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01565"
FT COILED 282..309
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 710 AA; 78806 MW; 7D334E143F3EDCEF CRC64;
MSSNATRTPV YFVSHGGPNI MYDTGHPAYT RLTALGREVT TKVKPKAILV LSAHWEGTAT
TLSINSAPST PLIYDFGGFP AHYYRAKYPH TGSPQLAQSA LRLLADAGIP AKPATRGLDH
GVWVPFSILF NPETNPLSIP VVQLSIFDSD SGDAHYALGE ALAPLRDEGV QIIVSGQAVH
NLPDFFASRG SLKPRDYTLT FDEALKEAVE VEPSERKGKM AELLKRGDAR KAHPTFEHLL
PVFVGAGAAK EDKGVRLWTM CEGSVSWGMF RFGDLPGESV GEKEAGEKIT KAEETYKKLL
NALDMMNLNI PDRENLLVSA IVRSRELSQA QEIVRLCNTF EIPIWSFSSG GDGDYRAAIP
RVPGSIGLGF GRYMNKVLGV NESGEYIVVQ PGATYADINQ YLVDNGLHQK FEPSWPEYMG
ESAIGNTAEG NMLTLYRGRE IILPNGDLPN TGKIQFPGIQ LTTDVLAQNG QLEIKENQRS
PSLHYELWDT SIRGPKPSYV SSNAPLNDVE LEDIDAYRWR LYGTVHGEKL ACNVLCQIIK
EEFAQIEGAK ISFVGGVQQE PSALSINEPE WTKWTPNGSY FSIMKQRFRE AGFDFVGTFT
IDQRQMHYVL YIMYERYDDA DSSRRVHKLI RTLMSDCAEN GWAEYCTYGA LMDQIAATRE
DPDDAMAKVN TAIRDAVDPT GSMEPDRNGI WSTRSDKSVW KRMADRSLVE
//
