ID K9ARZ8_9STAP Unreviewed; 289 AA.
AC K9ARZ8;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
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 ORFNames=C273_02408 {ECO:0000313|EMBL:EKU50084.1};
OS Staphylococcus massiliensis S46.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1229783 {ECO:0000313|EMBL:EKU50084.1, ECO:0000313|Proteomes:UP000009885};
RN [1] {ECO:0000313|EMBL:EKU50084.1, ECO:0000313|Proteomes:UP000009885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S46 {ECO:0000313|EMBL:EKU50084.1,
RC ECO:0000313|Proteomes:UP000009885};
RX PubMed=23929469;
RA Srivastav R., Singh A., Jangir P.K., Kumari C., Muduli S., Sharma R.;
RT "Genome Sequence of Staphylococcus massiliensis Strain S46, Isolated from
RT the Surface of Healthy Human Skin.";
RL Genome Announc. 1:e00553-13(2013).
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}.
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:EKU50084.1}.
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DR EMBL; AMSQ01000003; EKU50084.1; -; Genomic_DNA.
DR RefSeq; WP_009382307.1; NZ_AMSQ01000003.1.
DR AlphaFoldDB; K9ARZ8; -.
DR STRING; 1229783.C273_02408; -.
DR PATRIC; fig|1229783.3.peg.488; -.
DR eggNOG; COG1893; Bacteria.
DR OrthoDB; 9793586at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000009885; Unassembled WGS sequence.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) 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:SF42; 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:EKU50084.1};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000009885}.
FT DOMAIN 5..130
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 160..280
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 289 AA; 32627 MW; 486C48FEEDB22CFF CRC64;
MKTFAVIGPG AVGTTIAKAI QDSGLDLTLY GREDKNVILE DFSSGEETRL RVKALNQATE
HVDVIFIAVK APQLQSVLDD LPRLCHQDTC VVLCQNGMGQ LKHLSSYNAY HAVIYISGQK
SGDHITHYRD YDIHVQNTKT TSHLKATLQH SALNVHLSDD VARKQWYKLL VNIGINSVTA
YYAEPASVLK NKEAYHMTKA LIQEGFNVAV AQGIDFEDTI MTKIMRIYEG YPDEMGTSMY
YDIINKRPLE LEVIHGYVRR VAHINEVSTP TLNKVYHDLK DTEKRYLEV
//