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Database: UniProt
Entry: A0A015KMV6_RHIIW
LinkDB: A0A015KMV6_RHIIW
Original site: A0A015KMV6_RHIIW 
ID   A0A015KMV6_RHIIW        Unreviewed;       407 AA.
AC   A0A015KMV6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=RirG_101140 {ECO:0000313|EMBL:EXX68869.1};
OS   Rhizophagus irregularis (strain DAOM 197198w) (Glomus intraradices).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=1432141 {ECO:0000313|EMBL:EXX68869.1, ECO:0000313|Proteomes:UP000022910};
RN   [1] {ECO:0000313|EMBL:EXX68869.1, ECO:0000313|Proteomes:UP000022910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM197198w {ECO:0000313|Proteomes:UP000022910};
RA   Lin K., Geurts R., Zhang Z., Limpens E., Saunders D.G., Mu D., Pang E.,
RA   Cao H., Cha H., Lin T., Zhou Q., Shang Y., Li Y., Ivanov S., Sharma T.,
RA   Velzen R.V., Ruijter N.D., Aanen D.K., Win J., Kamoun S., Bisseling T.,
RA   Huang S.;
RT   "Single nucleus genome sequencing reveals high similarity among nuclei of
RT   an endomycorrhizal fungus.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:EXX68869.1}.
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DR   EMBL; JEMT01017087; EXX68869.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A015KMV6; -.
DR   HOGENOM; CLU_676439_0_0_1; -.
DR   OMA; GGWIAPH; -.
DR   Proteomes; UP000022910; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   PANTHER; PTHR43765:SF2; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000022910}.
FT   DOMAIN          4..198
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          221..343
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   COILED          74..101
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   407 AA;  47105 MW;  06CC9EAE1B119BD4 CRC64;
     MVAIAILGCG NVGFYIASHL IHNNHHAFNN PYNNNKILCV GRQRLLDELN LSKKLTLTKL
     NNFTDIDTVK ENNYLLKEND KIEAEDEKDE YEEKIVILRD EIFYETDLKE LIKFNPDYVI
     VTLKSNQISD VFNELKDLDG KTTIVSIQNS FHNAEIIKQF LPNTTIIRGL LNDMTVTHDS
     SCHFIQQSSS SGSIVLESIP ETLHFQKILE QNELPCVISY DIEDLMYFKL LINLNTSLFA
     LSGLSYVEYL QDNNFREIYK KCIFEGLNVY RLNGITFSEN LLMKNLVKCL GYVPEWVSDL
     ALEHFLITKK RNLNSSMVYD FKSARKTEVE FLQGEIVKLG ERIRSKDNQR EDVQHEKSVD
     VKYNRGILNL IKIIENHMIE SKKGWDGKIS DKEILKYIET GEVPNVL
//
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