ID A0A137P2X4_CONC2 Unreviewed; 524 AA.
AC A0A137P2X4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=FAD-binding domain-containing protein {ECO:0000313|EMBL:KXN69362.1};
GN ORFNames=CONCODRAFT_8220 {ECO:0000313|EMBL:KXN69362.1};
OS Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS (Delacroixia coronata).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC Ancylistaceae; Conidiobolus.
OX NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN69362.1, ECO:0000313|Proteomes:UP000070444};
RN [1] {ECO:0000313|EMBL:KXN69362.1, ECO:0000313|Proteomes:UP000070444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN69362.1,
RC ECO:0000313|Proteomes:UP000070444};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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; KQ964537; KXN69362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137P2X4; -.
DR STRING; 796925.A0A137P2X4; -.
DR EnsemblFungi; KXN69362; KXN69362; CONCODRAFT_8220.
DR OMA; YNEDWMR; -.
DR OrthoDB; 1664005at2759; -.
DR Proteomes; UP000070444; 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 Reference proteome {ECO:0000313|Proteomes:UP000070444}.
FT DOMAIN 85..264
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 524 AA; 57548 MW; 2B65AB752912AF88 CRC64;
MIKLNSILKL NKLVNNTTLI KSYSSKVIPL TKDRYTYLQR NPSYKSLEDS DLAHFKTIVG
EAGIQANLND VSELESHNAD WMGVYKGSSQ CVLKPNSTQQ VSEILKYCNE KKLAVVPQGG
NTGLVGGSVP VFDEVILSTN RLNKVRSFDN VSGVIVSDAG CILEQLNQYL EPEGYMMPLD
LGAKGSCHIG GNLATNAGGL RLLRYGSLHG TTLGLEVVLP DGTILDNLST LRKDNTGYDL
KQLFIGSEGT LGIITGASVL TPKIPKSVNV ALLGVNSYED VQKVFRNVRS DLLEILSAFE
FMDIDSFKVA LKHSNLPNPL SETYPFYVLI ETHGSNMDHD QEKLGLVLEN LLTEGLALDG
TLAQDQTQIG KIWSIRELIP EAIQHLGKPY KYDVSIPLPD LYNVVQIVKS KLADKGHYDP
TGKNTDALIR EVCGYGHIGD GNLHLNIVAK EASPKVNEIL EPFIFEVVQT FQGSISAEHG
LGLQKAKFIQ YSKSPTMIKT MQSVKKLLDP NNILNPYKYL PATN
//
