ID A0A178E948_9PLEO Unreviewed; 906 AA.
AC A0A178E948;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Aromatic compound dioxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=IQ07DRAFT_610434 {ECO:0000313|EMBL:OAL51613.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL51613.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL51613.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL51613.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR634183-3};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|ARBA:ARBA00001965};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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DR EMBL; KV441642; OAL51613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178E948; -.
DR STRING; 765867.A0A178E948; -.
DR InParanoid; A0A178E948; -.
DR OrthoDB; 275353at2759; -.
DR Proteomes; UP000077535; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0018576; F:catechol 1,2-dioxygenase activity; IEA:InterPro.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR GO; GO:0009712; P:catechol-containing compound metabolic process; IEA:InterPro.
DR GO; GO:1901565; P:organonitrogen compound catabolic process; IEA:UniProt.
DR CDD; cd01156; IVD; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 1.20.1290.10; AhpD-like; 1.
DR Gene3D; 2.60.130.10; Aromatic compound dioxygenase; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR029032; AhpD-like.
DR InterPro; IPR007535; Catechol_dOase_N.
DR InterPro; IPR003779; CMD-like.
DR InterPro; IPR000627; Intradiol_dOase_C.
DR InterPro; IPR015889; Intradiol_dOase_core.
DR InterPro; IPR034183; IVD.
DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF18; ISOVALERYL-COENZYME A DEHYDROGENASE; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF02627; CMD; 1.
DR Pfam; PF00775; Dioxygenase_C; 1.
DR Pfam; PF04444; Dioxygenase_N; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF69118; AhpD-like; 1.
DR SUPFAM; SSF49482; Aromatic compound dioxygenase; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR634183-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535}.
FT DOMAIN 33..103
FT /note="Catechol dioxygenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04444"
FT DOMAIN 116..293
FT /note="Intradiol ring-cleavage dioxygenases"
FT /evidence="ECO:0000259|Pfam:PF00775"
FT DOMAIN 372..444
FT /note="Carboxymuconolactone decarboxylase-like"
FT /evidence="ECO:0000259|Pfam:PF02627"
FT DOMAIN 526..635
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 639..734
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 746..897
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT ACT_SITE 759
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-1"
FT BINDING 640..649
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 649
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT BINDING 673..675
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 695..696
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT BINDING 757..760
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT BINDING 785
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 796
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 857..861
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 884..885
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT BINDING 886..888
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
SQ SEQUENCE 906 AA; 100332 MW; CF903255252909CD CRC64;
MSQAPNIQDA GKHRFDPNFT DAVIGAIGPN VPERRRFVLS SMIRHLHDFI REVELTNDEW
FEGVRFVNSI GKTTTNTRNE AHRISDVLGV ESLVDEIAHK HINESGEAPT SSTILGPFWS
PHSPFRDLGD SIVRNEHADG QKTLMHGVVR DLDTKKGIPN AVIDIWQASA NGKYDFQDPE
NQEPNNLRGK FTTNEKGEYW YYCYKPTAYS LPTDGAAGKL FEAMERHPFR PAHIHLMVSA
DNYKPLITQL YPRDDQYVTN DTVFAVKDDL LLDFKPSNDS KAKLDLEYNV TLAPAGKKTT
RLEGIPRLPN SHHSSRSTLT RTFTTASSLK MRVEYAPSEP QNEADRPIYE RIAERRKPRP
LIPLDLALLH NPAMADGWNS FIGAIRTKNS VPENLKELAI SRVAVLNKAV HEWDVHSALA
FNAGVSKEAL QTVFDLPVTR HGMAEREGLL GFRDEEYAVL VYTDQMTIGV EVEESVAEKL
KEYLSDKQIV ELTATIAAYN CVSSARRHAS TKHPANFTPP TQGDLDELRE SVREFARREI
PEELAAKTDK DNEFPNDMWK KFGEAGFLGI TADEEFGGLA MGYQAHCVVM EELSRASGSI
ALSYAAHSQL CVNQLMLNGS AAQKKKYLPG LISGEQIGAL AMSEHGAGSD VVSMKTTAKE
VDGGYVLNGT KMWITNGPDA HTIVVYAKTQ PDAASKGITA FIVETTAKGF SVAQKLDKLG
MRGSNTGELV FEDVFVPKEN VLGEVNRGVR VLMEGLDLER LVLSAGPLGL MQASLDNVLP
YTHQRKQFGT PIAHNQLVQG KLADMYTKYR ASQAFTYSIA RAVDESHASP DIRTQDCAGA
ILYAAERASE VAADAIQLMG GMGYMNEVPV GRILRDAKLY EIGAGTSEVR RMVIGRAFNK
EYKQEI
//
