ID A0A126Z534_9MICO Unreviewed; 298 AA.
AC A0A126Z534;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=AX769_16740 {ECO:0000313|EMBL:AMM21481.1};
OS Frondihabitans sp. PAMC 28766.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frondihabitans.
OX NCBI_TaxID=1795630 {ECO:0000313|EMBL:AMM21481.1, ECO:0000313|Proteomes:UP000070552};
RN [1] {ECO:0000313|EMBL:AMM21481.1, ECO:0000313|Proteomes:UP000070552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC28744 {ECO:0000313|Proteomes:UP000070552};
RA Park H.;
RT "Complete genome of Frondihabitans sp.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP014513; AMM21481.1; -; Genomic_DNA.
DR RefSeq; WP_066281648.1; NZ_CP014513.1.
DR AlphaFoldDB; A0A126Z534; -.
DR STRING; 1795630.AX769_16740; -.
DR KEGG; frp:AX769_16740; -.
DR OrthoDB; 8555723at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000070552; 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 Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000070552}.
FT DOMAIN 9..149
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 175..292
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 298 AA; 31376 MW; E91C07EB0BC6E432 CRC64;
MSATTTPTIA VVGPGAIGTT VAAALHEVGR TPRLFGRTAR DHLQLDVDDR HILVPGPVET
DPGRAGGPVD LVFLAVKTTQ IEAAAPWLAA LCGPDTVVCA LQNGVEQEAM VSPHAAGAQV
IPSVVWFPAQ AQPDGSVWLR GPARLTVPDT AAGRVVRDAL EGTRCTVELA ADFPSVAWRK
LLQNAVAGLQ ALTGRRAGMY ARADITELSL AYLRECLEVA RADGAVLTDD VPDEIVAYFQ
AFPPDVGTSI LVDREQGRPL EWDIRNGVVQ RRARARGILT PISDVLVPLL AAASDGPG
//
