ID G1X3L1_ARTOA Unreviewed; 606 AA.
AC G1X3L1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=AOL_s00043g284 {ECO:0000313|EMBL:EGX52495.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX52495.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX52495.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EGX52495.1}.
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DR EMBL; ADOT01000057; EGX52495.1; -; Genomic_DNA.
DR RefSeq; XP_011119073.1; XM_011120771.1.
DR AlphaFoldDB; G1X3L1; -.
DR STRING; 756982.G1X3L1; -.
DR GeneID; 22889980; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_024402_0_0_1; -.
DR InParanoid; G1X3L1; -.
DR OMA; VFYGTQY; -.
DR OrthoDB; 5474593at2759; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR016170; Cytok_DH_C_sf.
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; PTHR11748:SF114; ARYL-ALCOHOL OXIDASE VANILLYL-ALCOHOL OXIDASE (AFU_ORTHOLOGUE AFUA_3G09500)-RELATED; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 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 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784}.
FT DOMAIN 100..297
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 606 AA; 67709 MW; 10B92D93ED1A10E3 CRC64;
MVTKDSPIPT LHDTHSGTPV RLLSVAKEHK DRLYSNKTVP PSVPRKQEVP VLPPDVSRPA
FNIAISDLKR LLGDEHVEVN DKPLVDGWYM EQPNTHDAFH ILEQEDLVSC GTAYPGSTED
VQTIVKWANR HLIPVYPISM GRNLGYGGAA PRLRGSLLVD LGKRMNRVLN IDGHNASCLV
EPGVSYFALY EEVQKTGYPL WIDTPDLGGG SVVGNALDRG VGYTPYGDHF AVHCGMEIVL
PNGEVLRTGM GSLPGAEGTD NPCWQAFQHN YGPSVDGLFS QSNFGIVTKM GMWLMPATGH
QSFMFTFVRD DDFEAIIEAL RPLALNRVIG NVPQIRNVIQ ELAVTGKGRA EFYDKKTPMP
REVIREHAKK MPFGDVSWFF YGTVYGDDET RAKSLGIIKE AFKKIPGAKF NLPEDMPVGH
YLRDRVDVCS GKPVLRELDW LNWVPNAAHL FFSPIVPTKG RDARLVHELV TKLHKKWGFD
SFPTWCVLGR ELHYIANIVY DRADPDAKRR AICLMREMIG KAADEGYGEY RTHLIFQDQV
AATYGWNGQA LNKFVETIKD AVDPNSIIAP GRNGIWGHRY KGRGFEMLPG QEERKTLTGL
PPQAKL
//