ID A0A397UJQ8_9GLOM Unreviewed; 1034 AA.
AC A0A397UJQ8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
DE Flags: Fragment;
GN ORFNames=C2G38_1906023 {ECO:0000313|EMBL:RIB09019.1};
OS Gigaspora rosea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Gigasporaceae; Gigaspora.
OX NCBI_TaxID=44941 {ECO:0000313|EMBL:RIB09019.1, ECO:0000313|Proteomes:UP000266673};
RN [1] {ECO:0000313|EMBL:RIB09019.1, ECO:0000313|Proteomes:UP000266673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 194757 {ECO:0000313|EMBL:RIB09019.1,
RC ECO:0000313|Proteomes:UP000266673};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RIB09019.1}.
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; QKWP01001426; RIB09019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397UJQ8; -.
DR STRING; 44941.A0A397UJQ8; -.
DR Proteomes; UP000266673; Unassembled WGS sequence.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR CDD; cd06207; CyPoR_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR19384:SF109; SULFITE REDUCTASE [NADPH] FLAVOPROTEIN COMPONENT; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000266673}.
FT DOMAIN 651..880
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RIB09019.1"
FT NON_TER 1034
FT /evidence="ECO:0000313|EMBL:RIB09019.1"
SQ SEQUENCE 1034 AA; 115557 MW; 0E48640DA45C22C5 CRC64;
GGAKFVDNKT AVAHIAYALS DTIFIYPTMH SNYSGEQTLH WSAQNMKNAF GKVCNVIKMD
TRSGASLAIL GAASFAYSGK FVAFASSQSI VSMLPNLYTI SKERIPLTIH VSAHGFDDNM
NNIANYDALM ARDTGFGIIN SYSTQEMHDI ALITHLISAS TKTPFLHVFD GIKAACGNSL
LNLIPYAELL KLSKEISNPS NSPPSANTII IVDKIDSIMK RIGKLVGRHY RAFEYVGSRD
ANILLVSCGG ETAIVKETVK HLNDNGKKVG VIIVRLYRPW SEKHFLAMVP KTVKKVAVLE
QVSNGSHDMG SSLFNDVVAS MIDSWTGDKP QLIDAKYPMS KQFTPSTVNT LLQQLESGGN
IDFNIDPSSD NFQIQSTLNN IKRCIFWDVE SKGTLLSNQH IANVFTRHSK LKGSKVSSLS
TFDTFNNGGV VTTNLLFGNE LTDVLHDLKI DAEYISIHDT TLISKYDILA PAKEGAIVIL
NTNWTTDDLE TKLPNDFRYE AFKRKIKLYI IDANKVVHDL GMNVDDHISL ILQIAFLRLT
INEAKINCGL EDALLELYDG NNEKELSLIL HSAVQETDKA LTFVEPPPAW QILEKSEHTL
PSFINSNSFG KSIDLQLLVK PKLGSWHTAI RNALFKEAFG FSNIQRPDVG EKTFVITVSE
NRRLTPTSYD RYLFHIEFDV TGTGLKYDLG EALGVYGHND PKEVNEFLED YGLNPDDLIS
IPNKEGDKFE TKTIYQVFVQ ILDIFGRPAK RFYESLALYA TDENEKNRLL WIASSEGSVE
FKRRVAETIT YADLLYEFTS ARPPVEDLVQ IIAPIKPRHY SIASAQSVHP NSVHLLVVTV
EWETSAGKKR FGQCTRYLSG LKVGSQVVVS IKPSVMKLPP RDTQPVIMAG LGTGMAPFRA
FIEERAYRKS KGIEVGPMIL YFGSRNRSME YLYGEELEAY HTEGLLTYLR LAFSRDQPHK
VYIQHKMKDD AELLHQYLLK DEGWFYLCGP TWPVPDVKDA IVSSFVSAGE LSLGDASAAL
NKLKDLERYI LEVY
//