ID A2SHZ3_METPP Unreviewed; 336 AA.
AC A2SHZ3;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 89.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
DE EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN OrderedLocusNames=Mpe_A2226 {ECO:0000313|EMBL:ABM95182.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM95182.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM95182.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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 -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004994}.
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DR EMBL; CP000555; ABM95182.1; -; Genomic_DNA.
DR RefSeq; WP_011829819.1; NC_008825.1.
DR AlphaFoldDB; A2SHZ3; -.
DR STRING; 420662.Mpe_A2226; -.
DR KEGG; mpt:Mpe_A2226; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_6_1_4; -.
DR OMA; NLGYHSG; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000000366; 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; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:ABM95182.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000366}.
FT DOMAIN 3..106
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 198..316
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 336 AA; 36019 MW; C31EE490E5F53693 CRC64;
MKIAIVGAGA IGGYLGAKLA IAGEDVTFIA RNRNLEAIRA NGFRLQLEDG SEQHAPTAKA
VQRMAEAGPQ DAVLLTVKAH QVRDLLPDLR ELFGPQTMVV TMINGVPWWY FHKLGGPYDG
QALRSVDPDG LLAQHIEPER VIGSVVYPAA ELVAPGVVKV IEGNRFTLGE PDGSRSPRIE
ALSQAMIRAG FKSPVSKDIR GEIWVKLWGN LSFNPISALT HATLQDICRF PLSRELAARM
MGEAQAVGQK LGVEFKISLD KRIAGAEAVG AHKTSMLQDV ENGRALELEA LVGSVVELGR
ITDTPTPTID AIYAAASLLG KTLGDARGRL QVQPLA
//