ID A0A942RQ38_UNCIG Unreviewed; 345 AA.
AC A0A942RQ38;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 10.
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=KGZ58_11550 {ECO:0000313|EMBL:MBS4029253.1};
OS Ignavibacteriales bacterium.
OC Bacteria; Pseudomonadati; Ignavibacteriota; Ignavibacteria;
OC Ignavibacteriales.
OX NCBI_TaxID=2049428 {ECO:0000313|EMBL:MBS4029253.1, ECO:0000313|Proteomes:UP000678872};
RN [1] {ECO:0000313|EMBL:MBS4029253.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CROMO_A_84 {ECO:0000313|EMBL:MBS4029253.1};
RA Brazelton W.;
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBS4029253.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CROMO_A_84 {ECO:0000313|EMBL:MBS4029253.1};
RA Sabuda M., Putman L., Schrenk M.;
RT "Biogeochemical Gradients in a Serpentinization-influenced Aquifer:
RT Implications for Gas Exchange between the Subsurface and Atmosphere.";
RL Submitted (MAY-2021) 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 + 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:MBS4029253.1}.
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DR EMBL; JAGXRH010000201; MBS4029253.1; -; Genomic_DNA.
DR Proteomes; UP000678872; 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:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-KW.
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; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
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|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000678872}.
FT DOMAIN 26..178
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 207..324
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 345 AA; 38194 MW; DDE08CD82671BA52 CRC64;
MDSVFRLNDK IENALLTNQM LSSFKIAILG VGAIGGYFGG KLAAQYANSD DVEIIFIARG
ENEKAIRTNG LKLITAQGEH IIRPSLVTSK PEQVGVVDFV LCCVKSYDLE TSIAPLKPCI
SDKTIILPLL YGVDASERIK KLFPQANVWD GCVYIVSRLI APGVVEEKGS MNSLYFGSSR
LSGTKETLQQ VETIFRTANV NARISENIVQ TLWEKFLFIS PFATLTSFLN TNIGGIMSNE
QHKELLFTLL LEVKAIADAK KISLSDNVVE KTMEQFAKLP AETTSSMHSD FQKGKQTELE
ALTTYVVEQG NELNVATPNY ERMLKGLGLE SYYSNHKPQT KLFTN
//
