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Database: UniProt
Entry: A0A177DI01_ALTAL
LinkDB: A0A177DI01_ALTAL
Original site: A0A177DI01_ALTAL 
ID   A0A177DI01_ALTAL        Unreviewed;       556 AA.
AC   A0A177DI01;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:OAG18459.1};
GN   ORFNames=AA0117_g4494 {ECO:0000313|EMBL:RYN78622.1}, CC77DRAFT_1010416
GN   {ECO:0000313|EMBL:OAG18459.1};
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:OAG18459.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG18459.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG18459.1,
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.
RN   [2] {ECO:0000313|Proteomes:UP000291422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FERA 1177 {ECO:0000313|Proteomes:UP000291422};
RA   Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA   Harrison R.J., Clarkson J.P.;
RT   "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT   species group including apple and Asian pear pathotypes.";
RL   bioRxiv 0:0-0(2019).
RN   [3] {ECO:0000313|EMBL:RYN78622.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FERA 1177 {ECO:0000313|EMBL:RYN78622.1};
RA   Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA   Harrison R.J., Clarkson J.P.;
RT   "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT   species group including apple and Asian pear pathotypes.";
RL   J. ISSAAS 0:0-0(2019).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; KV441483; OAG18459.1; -; Genomic_DNA.
DR   EMBL; PDXD01000007; RYN78622.1; -; Genomic_DNA.
DR   RefSeq; XP_018383880.1; XM_018523649.1.
DR   GeneID; 29109243; -.
DR   KEGG; aalt:CC77DRAFT_1010416; -.
DR   VEuPathDB; FungiDB:CC77DRAFT_1010416; -.
DR   OMA; GPSYYIT; -.
DR   OrthoDB; 52047at2759; -.
DR   Proteomes; UP000077248; Unassembled WGS sequence.
DR   Proteomes; UP000291422; 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   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR47190:SF1; -; 1.
DR   PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 3.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..556
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5040669902"
FT   DOMAIN          286..300
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         247
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   556 AA;  59711 MW;  A532BD019B42A34C CRC64;
     MVASYMLKTL LPVAVLTSYA AAETCAGGEW DVIVVGSGPA GIVTADRMSE AGKKTLLLEQ
     GGPSYYVTGG RARPEWLNGT ELSRVDVPGL YKSIFSNSGE GNLTCASDVV NAFQGCTVGG
     NSAINAGLFF QPPASDWNRY FPDGWKDADM QSAIKKVRTK QPSTDSPSQD GKRYLQSGYE
     AAKRWLVDGA GYADVGLNDG IENHNKTKVF GHPIWYYENG QRSGPVKTYL QSALNRTNFS
     FQTGTKVLRV RRDGGVATGV DVQTNGASSS HSICIKKGGM VISSAGALLS PQLLMWSGIG
     EAETLKNLSK NGHVTVPSQE WINNTAVGNG VFDNPNTFIE LYSDEIASYS YSYSNPPPSD
     VELYLNNRSG PYTFASQTSA FWDYIEQGDD VVGCQGTIDS AGAMDLLENG TITLNVYGTS
     GLRSVGRVNL DARGIALPNS NFYSDPRDAA AIATFVHNIF QALPHTLTPL NIAKNSTLEQ
     ISTWLTTPSA YTRGNVQHWS SSCRMESCVD ANTKVIGMQN LFVIDASIVP PLTTNPVMGV
     MIAAERAVER ILALGK
//
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