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Database: UniProt
Entry: A0A367IYL2_RHIST
LinkDB: A0A367IYL2_RHIST
Original site: A0A367IYL2_RHIST 
ID   A0A367IYL2_RHIST        Unreviewed;       323 AA.
AC   A0A367IYL2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00013014, ECO:0000256|RuleBase:RU362068};
DE            EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014, ECO:0000256|RuleBase:RU362068};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024, ECO:0000256|RuleBase:RU362068};
GN   Name=PAN5_1 {ECO:0000313|EMBL:RCH82764.1};
GN   ORFNames=CU098_006976 {ECO:0000313|EMBL:RCH82764.1};
OS   Rhizopus stolonifer (Rhizopus nigricans).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=4846 {ECO:0000313|EMBL:RCH82764.1, ECO:0000313|Proteomes:UP000253551};
RN   [1] {ECO:0000313|EMBL:RCH82764.1, ECO:0000313|Proteomes:UP000253551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LSU 92-RS-03 {ECO:0000313|EMBL:RCH82764.1,
RC   ECO:0000313|Proteomes:UP000253551};
RX   PubMed=29674435; DOI=10.1534/g3.118.200235;
RA   Gryganskyi A.P., Golan J., Dolatabadi S., Mondo S., Robb S., Idnurm A.,
RA   Muszewska A., Steczkiewicz K., Masonjones S., Liao H.L., Gajdeczka M.T.,
RA   Anike F., Vuek A., Anishchenko I.M., Voigt K., de Hoog G.S., Smith M.E.,
RA   Heitman J., Vilgalys R., Stajich J.E.;
RT   "Phylogenetic and Phylogenomic Definition of Rhizopus Species.";
RL   G3 (Bethesda) 8:2007-2018(2018).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC       pantoic acid. {ECO:0000256|RuleBase:RU362068}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:16233, ChEBI:CHEBI:11561, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15980, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.169; Evidence={ECO:0000256|RuleBase:RU362068};
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
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:RCH82764.1}.
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DR   EMBL; PJQM01004986; RCH82764.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367IYL2; -.
DR   STRING; 4846.A0A367IYL2; -.
DR   EnsemblFungi; RCH82764; RCH82764; CU098_006976.
DR   Proteomes; UP000253551; Unassembled WGS sequence.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
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; IPR003710; ApbA.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00745; apbA_panE; 1.
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   NADP {ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253551}.
FT   DOMAIN          3..151
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          195..320
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   323 AA;  35893 MW;  D5A6EBC8033D691C CRC64;
     MNIHILGTGA IGCLLGASLK STNNKVTLLL RSKAHYEDFR NRQNSIIYRR DGQHQAISGF
     DASIADDTTD TSPISSLIVS TKANHTLKAL KPIASRLTPE STVLLLQNGM GVAEHLMENL
     WRDESKVPNV MVGVNRHAVQ RLAPYNIHHH SGYTDPNAFR IGKFPNSNPT QKSEMIDKIV
     AIPNFQAAVL PWKKLRKEML TKLFINSCIN GVASVLMCKN KGVIVNNNPG GVAMMRAICE
     EAYEVFKDDL PGETMESMMD VVLRVNKEAG ENTCSTLQDI QNRQITEIDY INGYICKMGN
     KMNINTKSNQ AIVNLIHARE ALY
//
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