ID A0A177DUZ7_ALTAL Unreviewed; 571 AA.
AC A0A177DUZ7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=CC77DRAFT_741863 {ECO:0000313|EMBL:OAG22619.1};
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:OAG22619.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG22619.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG22619.1,
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 -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV441474; OAG22619.1; -; Genomic_DNA.
DR RefSeq; XP_018388040.1; XM_018533012.1.
DR AlphaFoldDB; A0A177DUZ7; -.
DR STRING; 5599.A0A177DUZ7; -.
DR GeneID; 29118606; -.
DR KEGG; aalt:CC77DRAFT_741863; -.
DR VEuPathDB; FungiDB:CC77DRAFT_741863; -.
DR OMA; YNEDWMR; -.
DR OrthoDB; 1664005at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
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 PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248}.
FT DOMAIN 139..318
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 50..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 571 AA; 63003 MW; 362C02DE71BE21E8 CRC64;
MIISAAVALL PQSTIMASSA RLVSSLRRTA FSSRVASRYQ YLRPTSQVRW TGSTSASSEP
HQPDEHGGVK GPTASAQSIK FTSESYPHLQ RDSKFAKVSE EHVKYFQDLL GSDSAVIDGV
TKDASEDIEA FNSDWMRKFR GHTKVVLKPK STEEVSKILK YCNDNMLAIV PQGGNTGLVG
GSVPVFDEIV INMQRMNEIR SFDEVSGILV ADAGVILENA DNFLAEKNHI FPLDLGAKGS
CYIGGNVATN AGGLRLLRYG SFHGNVLGIE AVLPDGTVVD DLSTLRKNNT GYDLKQLFIG
GEGTIGIITK VSIICPRRSP AVNVAYFGLE SYEKVQKAYI EAKGHLSEIL SAFELMDGRT
QKLVNRVKGK KMPLEGEYPF YCLIETSGSN ADHDNEKLQA FLEHVMETEV VSDGVLAQDQ
TQIQELWSWR EGITECLGHD GGVYKYDLSI PIGELYDLVN ETRDRLTEAG LLGNDASHPV
VDVVGYGHMG DANLHLNIPV RKFDKSVEKQ LEPFVYEWVQ KRNGSISAEH GLGVTKKPYI
GYSKSETMIK LMKQIKDLYD PNGIMNPYKY I
//
