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Database: UniProt
Entry: U9UTX6_RHIID
LinkDB: U9UTX6_RHIID
Original site: U9UTX6_RHIID 
ID   U9UTX6_RHIID            Unreviewed;       563 AA.
AC   U9UTX6;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:POG71044.1};
GN   ORFNames=GLOIN_2v1611262 {ECO:0000313|EMBL:POG71044.1};
OS   Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS   (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=747089 {ECO:0000313|EMBL:POG71044.1, ECO:0000313|Proteomes:UP000018888};
RN   [1] {ECO:0000313|EMBL:POG71044.1, ECO:0000313|Proteomes:UP000018888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194
RC   {ECO:0000313|Proteomes:UP000018888};
RX   PubMed=24277808; DOI=10.1073/pnas.1313452110;
RA   Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA   Charron P., Duensing N., Frei Dit Frey N., Gianinazzi-Pearson V.,
RA   Gilbert L.B., Handa Y., Herr J.R., Hijri M., Koul R., Kawaguchi M.,
RA   Krajinski F., Lammers P.J., Masclaux F.G., Murat C., Morin E.,
RA   Ndikumana S., Pagni M., Petitpierre D., Requena N., Rosikiewicz P.,
RA   Riley R., Saito K., San Clemente H., Shapiro H., van Tuinen D., Becard G.,
RA   Bonfante P., Paszkowski U., Shachar-Hill Y.Y., Tuskan G.A., Young P.W.,
RA   Sanders I.R., Henrissat B., Rensing S.A., Grigoriev I.V., Corradi N.,
RA   Roux C., Martin F.;
RT   "Genome of an arbuscular mycorrhizal fungus provides insight into the
RT   oldest plant symbiosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:20117-20122(2013).
RN   [2] {ECO:0000313|EMBL:POG71044.1, ECO:0000313|Proteomes:UP000018888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194
RC   {ECO:0000313|Proteomes:UP000018888};
RX   PubMed=29355972;
RA   Chen E.C.H., Morin E., Beaudet D., Noel J., Yildirir G., Ndikumana S.,
RA   Charron P., St-Onge C., Giorgi J., Kruger M., Marton T., Ropars J.,
RA   Grigoriev I.V., Hainaut M., Henrissat B., Roux C., Martin F., Corradi N.;
RT   "High intraspecific genome diversity in the model arbuscular mycorrhizal
RT   symbiont Rhizophagus irregularis.";
RL   New Phytol. 0:0-0(2018).
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   -!- 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:POG71044.1}.
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DR   EMBL; AUPC02000113; POG71044.1; -; Genomic_DNA.
DR   AlphaFoldDB; U9UTX6; -.
DR   STRING; 747089.U9UTX6; -.
DR   VEuPathDB; FungiDB:GLOIN_2v1611262; -.
DR   eggNOG; KOG1232; Eukaryota.
DR   HOGENOM; CLU_017779_4_1_1; -.
DR   OrthoDB; 1664005at2759; -.
DR   Proteomes; UP000018888; 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:UP000018888}.
SQ   SEQUENCE   563 AA;  62438 MW;  37C814C7F2E2C013 CRC64;
     MVYTPNLISR QFFGKIVLTR SNYLKNFVVR NVNRNSIQFI VPTNRKFATS IESSTSGAEI
     PAKKHAPTKK VEFTADKYTY LHRNPNFKEL TQDDIKFFAS ILPANGLIID NEEELMPYNV
     DWMKKYRGKS RLVARPKTTR QISQILKYCN ENKLPVVPQG GNTGLVGGGV PVFDEIVIST
     NNMNQIRSFD PVSGILTCDA GCILEVLDNY LAEQEQGYMM PLDLGAKGSC HIGGNVATNA
     GGLRLLRYGS LHGTVLGLEA VLPDGTILDN LSTLRKDNTG YDIKQLFIGS EGTLGVITGV
     SILTPPKPKA VNVAVLGVST FQNVQKALVT SKNKLSEILS AFEFWDSDTL KLSKAHNIQG
     TKFPLEDNYP FYVLVEISGS NKYHDDDKLQ NFLEELLANE IVKDGVVAQD ETQMSTLWSL
     REGIPEACSK AGAVYKYDIS IPLSVFYQMA EDMRNRLQSA GVFGEDNLVS NVIAYGHVGD
     GNLHLNIVAK SYDPKVTNLI EPFIYEWTEQ HNGSISAEHG LGLMKANYLK YSKSSSMISI
     MKQIKQSIDP NGIMNPYKFL PTQ
//
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