ID A0A8J3EX50_9BIFI Unreviewed; 322 AA.
AC A0A8J3EX50;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 02-APR-2025, entry version 16.
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 ORFNames=GCM10007377_02630 {ECO:0000313|EMBL:GGI12772.1};
OS Galliscardovia ingluviei.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Galliscardovia.
OX NCBI_TaxID=1769422 {ECO:0000313|EMBL:GGI12772.1, ECO:0000313|Proteomes:UP000619536};
RN [1] {ECO:0000313|EMBL:GGI12772.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCM 8606 {ECO:0000313|EMBL:GGI12772.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [2] {ECO:0000313|EMBL:GGI12772.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCM 8606 {ECO:0000313|EMBL:GGI12772.1};
RA Sun Q., Sedlacek I.;
RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
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}.
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:GGI12772.1}.
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DR EMBL; BMDH01000001; GGI12772.1; -; Genomic_DNA.
DR RefSeq; WP_188354446.1; NZ_BMDH01000001.1.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000619536; Unassembled WGS sequence.
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 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:UP000619536}.
FT DOMAIN 3..146
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 186..310
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 322 AA; 36354 MW; 1F4C656047612664 CRC64;
MKYAVLGAGA MGLRYGILLQ KLAGKTVDFV DTWEPGIEAV RRQGGVYVSR DHENRHLVPI
EVYRPEEYTG NPDVWIIMLK QMQLEAVLKR CHDAGLFQDH QVVFSAMNGW GHFDHIRQYF
SEDRIYGGTA LVATVLNGPG DVDFIGKPGA GTMTLCSYTG DITEIERQMH DDLQQANFNP
TITQDLKGTC MAKVVFNSVV NTLCTMYQIQ MGQFISYPGA RDVARQLIDE AYDALERDGV
KLINTRDEEL ETVDYVSRTG NPLHYPSMYQ DMIHSRPTEV DYINGYIAAV GRKHGYVCHT
HEFLTHGVHL AELAHRLHET QA
//
