ID A0A177D576_ALTAL Unreviewed; 568 AA.
AC A0A177D576;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:OAG14843.1};
GN ORFNames=CC77DRAFT_1000505 {ECO:0000313|EMBL:OAG14843.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG14843.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG14843.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG14843.1,
RC ECO:0000313|Proteomes:UP000077248};
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:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; KV441497; OAG14843.1; -; Genomic_DNA.
DR RefSeq; XP_018380264.1; XM_018523123.1.
DR AlphaFoldDB; A0A177D576; -.
DR STRING; 5599.A0A177D576; -.
DR GeneID; 29108717; -.
DR KEGG; aalt:CC77DRAFT_1000505; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1000505; -.
DR OMA; IVACANK; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 4.10.450.10; Glucose Oxidase, domain 2; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027424; Glucose_Oxidase_domain_2.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF201; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248}.
FT DOMAIN 80..103
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 275..289
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 33..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 505
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 548
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 86
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 568 AA; 61612 MW; 99AA584B9760C249 CRC64;
MSADYVIVGG GTAGLVVANR LSANPNTRVV LIEPGEDDRN NPNVTDPLRR DENANTAIDW
SYKSTPQAQM NDRSVEFIAG KIVGGTSMIN GMMYIRAATA EINGWERLGA KGWNWNSLWP
FYKGLERFIN PTPEQSDSGI KVDPEFHGTN GDLAVSYPTQ LPTEHLSSAL ADTWETLGVP
TRSDANGGMV EGYTTRPMMI DSKSGVRASA AVAFYYPISD RKNLSLIQGT VLNLTWGDRT
EEDSLSADGC QYRDGDGKLH SVRLSEGGQI ILAAGALATP AILQASGVGS SSLLNDLGIQ
VQLDLPGVGE NLQDQPDLTF SYSPKNPTPD AITPYAAFVT AKDVFGEETE SMAASTEANL
RGWAEIVACA NKHVGPDAIE TIFRHQHGLI FKEKLAIGEI TMTSSTKMSS EYWSLLPFSR
GSVRLSSRAE DGTYEVDIDP RFFQIDFDQD CFTKLGRLVQ KFWSTAPAAE KVTSKIEPKN
EKLPDDASTE QWNSYVKEKT VANHHVLGTA AMMSRELGGV VDENLKVYGT RNVRVVDASV
IPMQVTGHLA STVYAVAARG ADLILNGN
//
