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Database: UniProt
Entry: A0A101FQS8_9FIRM
LinkDB: A0A101FQS8_9FIRM
Original site: A0A101FQS8_9FIRM 
ID   A0A101FQS8_9FIRM        Unreviewed;       320 AA.
AC   A0A101FQS8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
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   ORFNames=XD69_0484 {ECO:0000313|EMBL:KUK41474.1};
OS   Clostridia bacterium 62_21.
OC   Bacteria; Bacillota; Clostridia.
OX   NCBI_TaxID=1635276 {ECO:0000313|EMBL:KUK41474.1, ECO:0000313|Proteomes:UP000067139};
RN   [1] {ECO:0000313|EMBL:KUK41474.1, ECO:0000313|Proteomes:UP000067139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=62_21 {ECO:0000313|EMBL:KUK41474.1};
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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}.
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:KUK41474.1}.
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DR   EMBL; LGFR01000033; KUK41474.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101FQS8; -.
DR   PATRIC; fig|1635276.4.peg.1232; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000067139; 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: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}.
FT   DOMAIN          3..151
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          183..310
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   320 AA;  34500 MW;  70634397F0FBEE52 CRC64;
     MHILVFGAGA LGSVFGGLLA RAGNDVVLVG RPWHLDAVTR EGLLIEGIWG RHRVSNLRVV
     YDLAELRGPF ALILVTVKAY DTSVAARAIQ PFVGPDTLVV SLQNGLGNAE ILAASVGKEK
     CAAGRVIFGA EIVTPGRVQV TVCADDVVIG PALPQAGAAL RHSIARAVAI IKEAGIPCRA
     VEDVQPYLWA KAFYNCALNP LGALLGVNYG RVHDNPHTRR IMNGVIREAF AVAVSKGIKL
     PWQDADAYLD DFYTVLLPPT RDHRPSMLQD LERGRRTEID ALNGKIVAYG RETGTPTPYN
     EVLTNLVHFR EISGKEFASD
//
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