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Database: UniProt
Entry: K2K128_9PROT
LinkDB: K2K128_9PROT
Original site: K2K128_9PROT 
ID   K2K128_9PROT            Unreviewed;       314 AA.
AC   K2K128;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
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   ORFNames=P24_07764 {ECO:0000313|EMBL:EKE76524.1};
OS   Oceanibaculum indicum P24.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Thalassobaculaceae; Oceanibaculum.
OX   NCBI_TaxID=1207063 {ECO:0000313|EMBL:EKE76524.1, ECO:0000313|Proteomes:UP000006746};
RN   [1] {ECO:0000313|EMBL:EKE76524.1, ECO:0000313|Proteomes:UP000006746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P24 {ECO:0000313|EMBL:EKE76524.1,
RC   ECO:0000313|Proteomes:UP000006746};
RX   PubMed=23209207; DOI=10.1128/JB.01859-12;
RA   Lai Q., Shao Z.;
RT   "Genome Sequence of Oceanibaculum indicum Type Strain P24.";
RL   J. Bacteriol. 194:6942-6942(2012).
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}.
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:EKE76524.1}.
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DR   EMBL; AMRL01000007; EKE76524.1; -; Genomic_DNA.
DR   RefSeq; WP_008944162.1; NZ_AMRL01000007.1.
DR   AlphaFoldDB; K2K128; -.
DR   STRING; 1207063.P24_07764; -.
DR   eggNOG; COG1893; Bacteria.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000006746; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006746}.
FT   DOMAIN          3..151
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          179..303
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   314 AA;  32727 MW;  6BA96BC9F33A3680 CRC64;
     MKIAILGAGA MGSVYGAILA RAGDNDVWLV DRWKEHIDAI RANGLKVTGA SGDWLSPSKA
     TTDPAEVGMC ELVIVATKTR DIESALTGAR PMIGPETLVL SIQNGLGAYD ILVKTVSKDR
     LLLGIAGGFG ATIPTPGHVH HNGFEIVKIG ATVPDAQPAA ETVAKLWAEA GFRAEAAPDI
     QSMIWSKLIC NVTYSAVCGI TGLTIGQVME TPEAWRVASS CASEAFAVAR ARGIALSFDD
     PVAYVHKFGS AIPGAKPSLL LDRLAGRQGE IDFLNGAVAD EGAKLGVPTP TNAIVAGLVR
     AMEAHDMRPA SHKN
//
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