ID A0A926V1A6_9CYAN Unreviewed; 322 AA.
AC A0A926V1A6;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 12.
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=H6G02_09310 {ECO:0000313|EMBL:MBD2154708.1};
OS Leptolyngbya sp. FACHB-16.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Leptolyngbyales;
OC Leptolyngbyaceae; Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=2692800 {ECO:0000313|EMBL:MBD2154708.1, ECO:0000313|Proteomes:UP000624057};
RN [1] {ECO:0000313|EMBL:MBD2154708.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FACHB-16 {ECO:0000313|EMBL:MBD2154708.1};
RX PubMed=32943748;
RA Chen M.Y., Teng W.K., Zhao L., Hu C.X., Zhou Y.K., Han B.P., Song L.R.,
RA Shu W.S.;
RT "Comparative genomics reveals insights into cyanobacterial evolution and
RT habitat adaptation.";
RL ISME J. 0:0-0(2020).
RN [2] {ECO:0000313|EMBL:MBD2154708.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FACHB-16 {ECO:0000313|EMBL:MBD2154708.1};
RA Chen M., Teng W., Zhao L., Hu C., Zhou Y., Han B., Song L., Shu W.;
RL Submitted (AUG-2020) 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|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 -!- 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:MBD2154708.1}.
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DR EMBL; JACJPN010000075; MBD2154708.1; -; Genomic_DNA.
DR Proteomes; UP000624057; 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 NCBIfam; NF004887; PRK06249.1; 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 ECO:0000313|EMBL:MBD2154708.1};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000624057}.
FT DOMAIN 11..158
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 190..310
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 322 AA; 35650 MW; 5814F4951C5A6B37 CRC64;
MTTTNTSKFR YAVVGTGALG GFYGARLQQA GMELHYLLNR DYEHVKIHGL KVDSPDGNFV
LPQVNAYSNA ADMPACDVVI VALKTTQNHL LKEILPPIVK PDGVVLVLQN GLGVEAEAAR
IVGSDRVIGG LCFLCSNKAG PGHINHLDYK KITMGEYTGD NSPGGVSDRL KTIAADFEQA
GIPIEMAEDL VLARWKKLMW NIPFNGLSVV LDATTDYIMQ DLYARALAIR LMEEVQQGAA
TQGRHIPDEF LQVMLDHTDA MKPYRTSMKI DYDEKRPLEV EAMYGSPLRT AMSGGVSLPR
IEMLYQQLKF LDRHNRQVRA QS
//
