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Database: UniProt
Entry: A9HCI9_GLUDA
LinkDB: A9HCI9_GLUDA
Original site: A9HCI9_GLUDA 
ID   A9HCI9_GLUDA            Unreviewed;       297 AA.
AC   A9HCI9;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 83.
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};
GN   Name=apbA {ECO:0000313|EMBL:CAP54952.1};
GN   OrderedLocusNames=GDI1009 {ECO:0000313|EMBL:CAP54952.1};
OS   Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298
OS   / CIP 103539 / LMG 7603 / PAl5).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconacetobacter.
OX   NCBI_TaxID=272568 {ECO:0000313|EMBL:CAP54952.1, ECO:0000313|Proteomes:UP000001176};
RN   [1] {ECO:0000313|EMBL:CAP54952.1, ECO:0000313|Proteomes:UP000001176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 /
RC   PAl5 {ECO:0000313|Proteomes:UP000001176};
RX   PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA   Bertalan M., Albano R., Padua V., Rouws L., Rojas C., Hemerly A.,
RA   Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V.,
RA   Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.,
RA   Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F.,
RA   Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L.,
RA   Figueiredo D., Montano H., Junior J., Filho G., Flores V., Ferreira B.,
RA   Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J.,
RA   Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., Amaral G.,
RA   Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C.,
RA   Urmenyi T., Kruger W.V., Martins O., Baldani J.I., Ferreira P.C.;
RT   "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT   Gluconacetobacter diazotrophicus Pal5.";
RL   BMC Genomics 10:450-450(2009).
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|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}.
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DR   EMBL; AM889285; CAP54952.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9HCI9; -.
DR   KEGG; gdi:GDI1009; -.
DR   OMA; WEKWVFL; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000001176; 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:UP000001176}.
FT   DOMAIN          2..132
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          160..275
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   297 AA;  31577 MW;  799CEE107A6C687B CRC64;
     MATAGHDVTF LVRPNRLQQL RTDGLRLVSP LGDASLAPKM VTSDDIDGPY DIILLSVKAY
     SLASAMDDFA AAVGPDTRII PLLNGMRHLD VLAERFGDPK VLGGTCFIVS KLDSEGHVVQ
     VGSLPKLTFG PRSSGDNAPI RSLKDALSGP GFETILSDHI IQEMWNKWAL LASLGTVCCL
     MRATVGEVAS APAGEAFARA TIGECASIAA AAGYPLTEET LGGIVRLLIA KESSLTSSMF
     RDLSQGAPIE ATQIIGDLVK RARAHQIATP TLDLINLNLT VYEQRRLRVS SVAEQSI
//
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