ID C8WUQ2_ALIAD Unreviewed; 311 AA.
AC C8WUQ2;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
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=Aaci_2865 {ECO:0000313|EMBL:ACV59869.1};
OS Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 /
OS DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 /
OS NRRL B-14509 / 104-IA) (Bacillus acidocaldarius).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=521098 {ECO:0000313|EMBL:ACV59869.1, ECO:0000313|Proteomes:UP000001917};
RN [1] {ECO:0000313|Proteomes:UP000001917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC
RC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA
RC {ECO:0000313|Proteomes:UP000001917};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Chertkov O., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Alicyclobacillus acidocaldarius subsp.
RT acidocaldarius DSM 446.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACV59869.1, ECO:0000313|Proteomes:UP000001917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC
RC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA
RC {ECO:0000313|Proteomes:UP000001917};
RX PubMed=21304673; DOI=10.4056/sigs.591104;
RA Mavromatis K., Sikorski J., Lapidus A., Glavina Del Rio T., Copeland A.,
RA Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L.,
RA Pitluck S., Ivanova N., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Meincke L.,
RA Sims D., Chertkov O., Han C., Brettin T., Detter J.C., Wahrenburg C.,
RA Rohde M., Pukall R., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Alicyclobacillus acidocaldarius type strain
RT (104-IA).";
RL Stand. Genomic Sci. 2:9-18(2010).
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; CP001727; ACV59869.1; -; Genomic_DNA.
DR RefSeq; WP_012812070.1; NC_013205.1.
DR AlphaFoldDB; C8WUQ2; -.
DR STRING; 521098.Aaci_2865; -.
DR KEGG; aac:Aaci_2865; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_6_0_9; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000001917; 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 ECO:0000313|EMBL:ACV59869.1};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000001917}.
FT DOMAIN 8..150
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 177..297
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 311 AA; 34062 MW; 5EFEB873EF6398C0 CRC64;
MTRVRRVTLV GLGAIGASYG ERLLAAPGVE LRVLVDEERK RRYEQSGVHV NGRRIDFPLA
VPADAVEPAD LVLFCVKYDD LAEAIEMVRG HVGPNTIFMS LLNGIASEED IQAAFPHHVV
LHAISVAIDA VREGRDVTYS TLGYISFGDA TGRHADAVRA VRDVFDRAGI AYETPDDILR
VVWWKFMINV GINQASAVLR APYGVFQQSE DAREVMRMAM REVVAIAQKG GISLTEEDVR
GFDDILNAMS PSGKTSMLQD VEAGRPTEVE QFAGKVVELG EQLGVPTPIN RLLYHAILSI
APHERMPCAS V
//
