ID A0A8D5ZPE1_9BACL Unreviewed; 310 AA.
AC A0A8D5ZPE1;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 02-APR-2025, entry version 15.
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=panE {ECO:0000313|EMBL:BCU82263.1};
GN ORFNames=JIR001_20460 {ECO:0000313|EMBL:BCU82263.1};
OS Polycladomyces abyssicola.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
OC Thermoactinomycetaceae; Polycladomyces.
OX NCBI_TaxID=1125966 {ECO:0000313|EMBL:BCU82263.1, ECO:0000313|Proteomes:UP000677436};
RN [1] {ECO:0000313|EMBL:BCU82263.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JIR-001 {ECO:0000313|EMBL:BCU82263.1};
RA Tsubouchi T., Shimane Y., Mori K., Usui K., Hiraki T., Tame A., Uematsu K.,
RA Maruyama T., Hatada Y.;
RT "Polycladomyces abyssicola gen. nov., sp. nov., a thermophilic filamentous
RT bacterium isolated from hemipelagic sediment.";
RL Int. J. Syst. Evol. Microbiol. 63:1972-1981(2013).
RN [2] {ECO:0000313|EMBL:BCU82263.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JIR-001 {ECO:0000313|EMBL:BCU82263.1};
RA Tsubouchi T., Kaneko Y.;
RT "Complete Genome Sequence of Polycladomyces abyssicola JIR-001T, Isolated
RT from Hemipelagic Sediment in Deep Seawater.";
RL Microbiol. Resour. Announc. 10:e00435-21(2021).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|ARBA:ARBA00002919,
CC ECO:0000256|RuleBase:RU362068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH + H(+);
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:ARBA00048793,
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; AP024601; BCU82263.1; -; Genomic_DNA.
DR RefSeq; WP_212772619.1; NZ_AP024601.1.
DR KEGG; pabs:JIR001_20460; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000677436; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
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; IPR050838; Ketopantoate_reductase.
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; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 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|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362068};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000677436}.
FT DOMAIN 3..151
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 181..305
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 310 AA; 34294 MW; BD2C7E8ED169BF43 CRC64;
MRIGVWGGGS LGLLWAARLA ALYPETVLVT RTREQADAVR NKGIRVIGLD GKVERIPVQA
VESDQATASF DVIMLMVKQR DFTSAFHQAI SACTPDGVIV CWQNGVGHDA VVKETNHTQA
VYGAVTTEGA WRESMTAVRH TGAGKTWMGP LLEKREDHPS SLQSLIVQVD RQWCPVALVD
DIQPRIWKKV IINSVINPLT ALLEVKNGEL LRLKGTGALI RSALEEGVAV VRAKGFRWEV
DDIFHEVEEV CGKTASNRSS MYQDVMRGHV TEIDWINGGI VKEGCAHGIP TPIHETLMRL
IHAKEERNRR
//
