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Database: UniProt
Entry: C6E1I9_GEOSM
LinkDB: C6E1I9_GEOSM
Original site: C6E1I9_GEOSM 
ID   C6E1I9_GEOSM            Unreviewed;       307 AA.
AC   C6E1I9;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|RuleBase:RU362068};
DE            EC=1.1.1.169 {ECO:0000256|RuleBase:RU362068};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|RuleBase:RU362068};
GN   OrderedLocusNames=GM21_0839 {ECO:0000313|EMBL:ACT16908.1};
OS   Geobacter sp. (strain M21).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=443144 {ECO:0000313|EMBL:ACT16908.1};
RN   [1] {ECO:0000313|EMBL:ACT16908.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M21 {ECO:0000313|EMBL:ACT16908.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Lovley D.;
RT   "Complete sequence of Geobacter sp. M21.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {ECO:0000256|RuleBase:RU362068}.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
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DR   EMBL; CP001661; ACT16908.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6E1I9; -.
DR   STRING; 443144.GM21_0839; -.
DR   KEGG; gem:GM21_0839; -.
DR   eggNOG; COG1893; Bacteria.
DR   HOGENOM; CLU_031468_6_0_7; -.
DR   OMA; WEKWVFL; -.
DR   OrthoDB; 5333395at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
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; PTHR21708:SF26; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 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   ECO:0000313|EMBL:ACT16908.1};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068}.
FT   DOMAIN          9..151
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          179..301
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   307 AA;  33329 MW;  E9B32A401F4FBAE8 CRC64;
     MGESKYKTTI IGAGALGAVY GSLLFDMDPD CVCFVAGGER HYRLKNDGVT VNGKRYAITV
     VKPEEATSAD LVIVAVKHHH LDEAIADMRK TVGLNTVILS VMNGIDSEER IGAAYGMEKV
     LYGLSLGIDA VREGGAVTYK NLGRILFGER ENKESTERVR RIASLFTRAG IAHEVPPDMV
     RSLWFKYMIN VGVNQVSAVL GETYGALRNS AEARELMDAA MREVIAVAVA KKVNLSEDDI
     GEWYKVLATL SAEGKTSMLQ DVEAGRKTEV EMLAGTVIEL GGRCGIPTPV NRKLFDDLKG
     IESSQAR
//
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