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Database: UniProt
Entry: A8MAY0_CALMQ
LinkDB: A8MAY0_CALMQ
Original site: A8MAY0_CALMQ 
ID   A8MAY0_CALMQ            Unreviewed;       278 AA.
AC   A8MAY0;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00013014, 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};
GN   OrderedLocusNames=Cmaq_1786 {ECO:0000313|EMBL:ABW02609.1};
OS   Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS   IC-167).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Caldivirga.
OX   NCBI_TaxID=397948 {ECO:0000313|EMBL:ABW02609.1, ECO:0000313|Proteomes:UP000001137};
RN   [1] {ECO:0000313|EMBL:ABW02609.1, ECO:0000313|Proteomes:UP000001137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167
RC   {ECO:0000313|Proteomes:UP000001137};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Caldivirga maquilingensis IC-167.";
RL   Submitted (OCT-2007) 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 + NAD(+) = 2-dehydropantoate + H(+) + NADH;
CC         Xref=Rhea:RHEA:61292, ChEBI:CHEBI:11561, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15980, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000256|ARBA:ARBA00000108};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:61294;
CC         Evidence={ECO:0000256|ARBA:ARBA00000108};
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:ARBA00000825};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16235;
CC         Evidence={ECO:0000256|ARBA:ARBA00000825};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004724, 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; CP000852; ABW02609.1; -; Genomic_DNA.
DR   RefSeq; WP_012186828.1; NC_009954.1.
DR   AlphaFoldDB; A8MAY0; -.
DR   STRING; 397948.Cmaq_1786; -.
DR   GeneID; 5709576; -.
DR   KEGG; cma:Cmaq_1786; -.
DR   eggNOG; arCOG04139; Archaea.
DR   HOGENOM; CLU_031468_0_0_2; -.
DR   OMA; NYSSMYQ; -.
DR   OrthoDB; 201845at2157; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000001137; Chromosome.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
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   Coenzyme A biosynthesis {ECO:0000256|RuleBase:RU362068};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001137}.
FT   DOMAIN          3..127
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          151..270
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   278 AA;  30231 MW;  A4FE7E97A828E6DD CRC64;
     MFSIIGLGAV GSLLTYFLNR AGFTPYVITR TLYDRYIIRL NGDYDLSIKL VQELPSEVKY
     TLIAVKAYDT VNVINKIKGT PVVFQNGIGG LELIKERLGV GYSAVVTYGV TRHGNITEVK
     GLGEIIMPSA LGELADILRS GGANVVVVDD VEPFRWLKVI VNAAINPITT ILKSPNGILI
     NNELARELAL EVINEGVAVV KALGINLPRD PVAETLDVAS KTSNNYSSML QDLMNCRETE
     IDYINGAITK YGSLLGIPTP INKALLIIIK ILRSLCLK
//
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