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Database: UniProt
Entry: A1HPU2_9FIRM
LinkDB: A1HPU2_9FIRM
Original site: A1HPU2_9FIRM 
ID   A1HPU2_9FIRM            Unreviewed;       306 AA.
AC   A1HPU2;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465, 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};
DE   Flags: Precursor;
GN   ORFNames=TcarDRAFT_1939 {ECO:0000313|EMBL:EAX48061.1};
OS   Thermosinus carboxydivorans Nor1.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Thermosinus.
OX   NCBI_TaxID=401526 {ECO:0000313|EMBL:EAX48061.1, ECO:0000313|Proteomes:UP000005139};
RN   [1] {ECO:0000313|EMBL:EAX48061.1, ECO:0000313|Proteomes:UP000005139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nor1 {ECO:0000313|EMBL:EAX48061.1,
RC   ECO:0000313|Proteomes:UP000005139};
RG   US DOE Joint Genome Institute (JGI-ORNL);
RA   Larimer F., Land M., Hauser L.;
RT   "Annotation of the draft genome assembly of Thermosinus carboxydivorans
RT   Nor1.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAX48061.1, ECO:0000313|Proteomes:UP000005139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nor1 {ECO:0000313|EMBL:EAX48061.1,
RC   ECO:0000313|Proteomes:UP000005139};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Pitluck S., Richardson P.;
RT   "Sequencing of the draft genome and assembly of Thermosinus carboxydivorans
RT   Nor1.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC       pantoic acid. {ECO:0000256|ARBA:ARBA00002919,
CC       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|ARBA:ARBA00000784,
CC         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|ARBA:ARBA00004994, 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:EAX48061.1}.
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DR   EMBL; AAWL01000005; EAX48061.1; -; Genomic_DNA.
DR   RefSeq; WP_007289046.1; NZ_AAWL01000005.1.
DR   AlphaFoldDB; A1HPU2; -.
DR   eggNOG; COG1893; Bacteria.
DR   OrthoDB; 9793586at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000005139; 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; 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|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362068};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005139}.
FT   DOMAIN          3..151
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          177..301
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   306 AA;  31707 MW;  037C5BC8B49B238A CRC64;
     MKIAIIGAGA MGSLFGGRLA QAGEDVWLLD VWEEHVAAIQ AHGLTLVDTT AETSIRLNAT
     TQADDIGPVD LVIIFVKSYA TPDAAQTAAA LLGPATTVLT LQNGLGNAET LAKVLGAERV
     VVGTTAMGAT LLGPGRIKCG GQGPTHIGSF SGGANPRLHD IATIFARAGI HTVVDSNVTA
     LVWSKLIINV GINAITALTG IPNGQVMASA ETRELVRLAV AEAVAVARAS GIPLPHTNYF
     DQVATVAQAT RDNRSSMLQD VTNRRRTEID AINGAIVAAG KRLGVPTPVN ETLTLLIKTL
     EQTYLS
//
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