ID A0A2U3PHM4_9MYCO Unreviewed; 268 AA.
AC A0A2U3PHM4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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};
DE Flags: Fragment;
GN ORFNames=MNAB215_5488 {ECO:0000313|EMBL:SPM43266.1};
OS Mycobacterium numidiamassiliense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1841861 {ECO:0000313|EMBL:SPM43266.1, ECO:0000313|Proteomes:UP000240424};
RN [1] {ECO:0000313|EMBL:SPM43266.1, ECO:0000313|Proteomes:UP000240424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB215 {ECO:0000313|EMBL:SPM43266.1,
RC ECO:0000313|Proteomes:UP000240424};
RG Urmite Genomes;
RL Submitted (JAN-2017) 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}.
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DR EMBL; FUEZ01000004; SPM43266.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U3PHM4; -.
DR STRING; 1841861.GCA_900157365_03807; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000240424; Unassembled WGS sequence.
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:UP000240424}.
FT DOMAIN 22..119
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 142..262
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:SPM43266.1"
SQ SEQUENCE 268 AA; 28351 MW; 752EF2C5EE74415E CRC64;
VLVCGRTPRD SIELRPDGQN PIVVPGPVHT DPAQVAGPAD FVVLAVKATQ NEDAAAWLAR
LCDGHTIVAV LQNGVEQVEQ VQPLCPSSPV VPGIVWYSAE TQPPGWVRLR TEAALVLPAG
PQAEALAELL RGAGCRVDND PDFITAAWRK LLTNALAGFM ALSGRRSGMF RRDDVAALSR
EYVAECLAVA RAEGAQLPDG VVDELVGLFR AAPVDMGTSI LADRVSNRPM EWDLRNGVIA
RKGRAHNLAT PISDVLVPLL AAASDGPG
//
