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Database: UniProt
Entry: F7V2Q0_CLOSS
LinkDB: F7V2Q0_CLOSS
Original site: F7V2Q0_CLOSS 
ID   F7V2Q0_CLOSS            Unreviewed;       342 AA.
AC   F7V2Q0;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
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=CXIVA_10620 {ECO:0000313|EMBL:BAK47029.1};
OS   Clostridium sp. (strain SY8519).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1042156 {ECO:0000313|EMBL:BAK47029.1, ECO:0000313|Proteomes:UP000008937};
RN   [1] {ECO:0000313|Proteomes:UP000008937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY8519 {ECO:0000313|Proteomes:UP000008937};
RX   PubMed=21914882; DOI=10.1128/JB.05637-11;
RA   Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT   "Complete genomic sequence of the O-desmethylangolensin-producing bacterium
RT   Clostridium rRNA cluster XIVa strain SY8519, isolated from adult human
RT   intestine.";
RL   J. Bacteriol. 193:5568-5569(2011).
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; AP012212; BAK47029.1; -; Genomic_DNA.
DR   RefSeq; WP_013976995.1; NC_015737.1.
DR   AlphaFoldDB; F7V2Q0; -.
DR   STRING; 1042156.CXIVA_10620; -.
DR   KEGG; cls:CXIVA_10620; -.
DR   eggNOG; COG1893; Bacteria.
DR   HOGENOM; CLU_031468_0_0_9; -.
DR   OMA; VVRWGQR; -.
DR   OrthoDB; 9793586at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000008937; Chromosome.
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   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008937}.
FT   DOMAIN          5..140
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          185..324
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   342 AA;  37660 MW;  4513EA372211C47F CRC64;
     MIKRIAIMGC GSLGTILGAY LSRAGLDVTM VDIWEEHVNT LNTQGASVSG GTEMTVPVKA
     CTPDQMTGTF DLFFYMTKQT FNETAIPQMI QHCGTDSIIC TCQNGLPELA VAEYYPKEKI
     MGATVGWPAT FLGPGKSKLT CPTDSPLFEF HLGRLTGEPD GTLHEVQQIL EKMCPGHVTI
     TSHLLADRWS KIMINATFSG MSTVCADTFA AVINNDRSMI CAARIGRECI RVCHAMDITL
     PSIFGINFNQ LFQFTDQAEE QHAVEVIRKY FGTIAGKASM LQDLEKGRKC EIRFINGVVS
     QYAKKYKIET PYNDSVVKIV SEIESGTRPL QNNLDSMPNL SL
//
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