ID A0A0N1HEE8_9EURO Unreviewed; 313 AA.
AC A0A0N1HEE8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=4,5-DOPA dioxygenase extradiol {ECO:0000313|EMBL:KPI43776.1};
GN ORFNames=AB675_6157 {ECO:0000313|EMBL:KPI43776.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI43776.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI43776.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI43776.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KPI43776.1}.
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DR EMBL; LFJN01000004; KPI43776.1; -; Genomic_DNA.
DR RefSeq; XP_018003739.1; XM_018146426.1.
DR AlphaFoldDB; A0A0N1HEE8; -.
DR STRING; 1664694.A0A0N1HEE8; -.
DR GeneID; 28738306; -.
DR OrthoDB; 1044515at2759; -.
DR Proteomes; UP000038010; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0008198; F:ferrous iron 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; 3.40.830.10; LigB-like; 1.
DR InterPro; IPR014436; Extradiol_dOase_DODA.
DR InterPro; IPR004183; Xdiol_dOase_suB.
DR PANTHER; PTHR30096:SF1; AROMATIC RING-OPENING DIOXYGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_7G00640); 1.
DR PANTHER; PTHR30096; UNCHARACTERIZED; 1.
DR Pfam; PF02900; LigB; 1.
DR PIRSF; PIRSF006157; Doxgns_DODA; 1.
DR SUPFAM; SSF53213; LigB-like; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000313|EMBL:KPI43776.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000038010};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 9..256
FT /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT subunit B"
FT /evidence="ECO:0000259|Pfam:PF02900"
SQ SEQUENCE 313 AA; 34615 MW; 4E6861D343104BE6 CRC64;
MGLPGLTPVH FFSHGSTRML EAETESGNYW AKCGQEALAH NVKGIVMMGA HWACLGDKIE
VATNPNPGKS PCPYVTPSLY LDWKPNPDLA TAERCISMLK ADGFNVGPNP NFDWIHDTFL
ILIKMFPDFS KCPPVTIVSM NARFDPHYHV KVGATLRPLR KEGYLLIGTG GAVHNLYRNA
WTDMILYRES LGQERPPEAW ALEFRQATED VVTRNRGPDL RKAMIRLMQH PAYRQAQATD
DHFMPAMFAA GAAGDLEDRA HANVLAAETW ELINMCNSQF TFGSYQASAD TSRKMLAKPH
KVASPAIAVA ASA
//
