ID C0QTN8_PERMH Unreviewed; 314 AA.
AC C0QTN8;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 82.
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 Name=panE {ECO:0000313|EMBL:ACO03216.1};
GN OrderedLocusNames=PERMA_0258 {ECO:0000313|EMBL:ACO03216.1};
OS Persephonella marina (strain DSM 14350 / EX-H1).
OC Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae;
OC Persephonella.
OX NCBI_TaxID=123214 {ECO:0000313|EMBL:ACO03216.1, ECO:0000313|Proteomes:UP000001366};
RN [1] {ECO:0000313|EMBL:ACO03216.1, ECO:0000313|Proteomes:UP000001366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14350 / EX-H1 {ECO:0000313|Proteomes:UP000001366};
RX PubMed=19136599; DOI=10.1128/JB.01645-08;
RA Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(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|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}.
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DR EMBL; CP001230; ACO03216.1; -; Genomic_DNA.
DR RefSeq; WP_012675455.1; NC_012440.1.
DR AlphaFoldDB; C0QTN8; -.
DR STRING; 123214.PERMA_0258; -.
DR PaxDb; 123214-PERMA_0258; -.
DR KEGG; pmx:PERMA_0258; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_0_0_0; -.
DR OMA; WEKWVFL; -.
DR OrthoDB; 9793586at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000001366; 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 ECO:0000313|EMBL:ACO03216.1};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000001366}.
FT DOMAIN 3..152
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 181..309
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 314 AA; 35200 MW; FD7B4AE4A492A459 CRC64;
MNIVVFGLGA VGTVFATFLK EAGYKVYGIT KDKYLNDLKS SELRVKGIWG DHRVKLDGIF
SSVSPLKDKK IDLIILSVKS YDTQNAVKSL KDMVSEKTKV IVAQNGYGNY EIVSEEIGKE
HTLLARVIFG SKIIKPGFAE VTVNADDVRI GDPSGTIPEE EIIKIACIIK NAGIPASYDP
DVYKTLWYKI LYNCALNPLG ALLSCSYGDL AENEETRKIM NRVIKEIFEV TEAHGIELNY
ESPEEYIEHF YKNLIPPTRN HYPSMYYDLK AGKKTEIDAL NGAIVRLARE KDIYVPVNET
ITGMIKFIEG RLRG
//