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Database: UniProt
Entry: A0A2H5S821_RHIID
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ID   A0A2H5S821_RHIID        Unreviewed;       418 AA.
AC   A0A2H5S821;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   02-APR-2025, entry version 30.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:POG70996.1};
GN   ORFNames=GLOIN_2v1610568 {ECO:0000313|EMBL:POG70996.1};
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:POG70996.1, ECO:0000313|Proteomes:UP000018888};
RN   [1] {ECO:0000313|EMBL:POG70996.1, 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:POG70996.1, 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. 220:1161-1171(2018).
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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:POG70996.1}.
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DR   EMBL; AUPC02000113; POG70996.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H5S821; -.
DR   SMR; A0A2H5S821; -.
DR   STRING; 747089.A0A2H5S821; -.
DR   VEuPathDB; FungiDB:RhiirFUN_018011; -.
DR   Proteomes; UP000018888; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:TreeGrafter.
DR   GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR   Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR050838; Ketopantoate_reductase.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018888}.
FT   DOMAIN          5..183
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          273..401
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          198..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   418 AA;  48264 MW;  9E16B63AB978805C CRC64;
     MVARWHVLGV GNYGSLFAHF LRKNGNKVTL LIRDPTTLNM FNKLNRTIEV TKEFEPEVEV
     TKGYQAECLQ GDYGNVIDPQ YPNELCPPHL RISKLIVTLK SHEFSKYYQR IFHRLSPTST
     IVLFTYGLGS YEELMRDYYS FDEASRPNII IALNSHHAYK KAKFGSQFKL IHSGFGEIDL
     GIVPRRFDEI KEKELNINSQ SLEDNNEDLD EISLPNEKMD NKTEESKTIT AATEADDDDN
     KGSEIEVDTL KSVIRSFSRI PELNARCVKY VNLINRKLEN LALNAVIDPL TSIYSIRNGA
     LLFNKVAEQT MRPICEETSI VIRKHREYLG MKPSNRFAPE RLIDAVFQIC IKTRHYESVM
     LQDVKKNFLT DIDYLNGYIV KLGKFYDIPT PINKFLIDMV KIRHNLQTNP KVLDELLK
//
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