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Database: UniProt
Entry: A0A1B8UXH9_9BACL
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ID   A0A1B8UXH9_9BACL        Unreviewed;       329 AA.
AC   A0A1B8UXH9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=BBG47_03335 {ECO:0000313|EMBL:OBY81103.1};
OS   Paenibacillus sp. KS1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1849249 {ECO:0000313|EMBL:OBY81103.1, ECO:0000313|Proteomes:UP000092663};
RN   [1] {ECO:0000313|EMBL:OBY81103.1, ECO:0000313|Proteomes:UP000092663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KS1 {ECO:0000313|EMBL:OBY81103.1,
RC   ECO:0000313|Proteomes:UP000092663};
RA   Lata P., Govindarajan S., Qi F., Li J.-L., Sahoo M.K.;
RT   "Deep sequencing identified Paenibacillus in Kanamycin resistant culture
RT   isolate from epiphyte Tillandsia usneoides (Spanish moss) in central
RT   Florida, USA.";
RL   Submitted (JUN-2016) 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 + 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|ARBA:ARBA00000784,
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:OBY81103.1}.
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DR   EMBL; MAIS01000005; OBY81103.1; -; Genomic_DNA.
DR   RefSeq; WP_065290509.1; NZ_MAIS01000005.1.
DR   AlphaFoldDB; A0A1B8UXH9; -.
DR   OrthoDB; 9800163at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000092663; 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; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   PANTHER; PTHR43765:SF2; 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|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092663}.
FT   DOMAIN          4..169
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          204..324
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   329 AA;  36924 MW;  522775DF5026E81F CRC64;
     MVIDIIGGGS LGLLHAAMLM RTRNSIDSSN TKVRMWTRTP EQAELIRSQG IHLEDLDGRQ
     AHIYPVHAYP LAEAGEVLER TGMRASSIWL FVKQTHIDSE LLSQLEKFPR EQTASLVCYQ
     NGVGHMEALS AIWPHEQLIW AVTTEAAKRV NCNEVVHTGH GHTSIGIWEP AGSRTEQKEL
     VNPLCLSTKK LLENAGFQTF LSNNIEGMVY QKLLVNVIIN PLTAVLRIKN GQLLLQEDRL
     SLMKELFGEA AAVYRAAHIS IDEEKDWERV VQVCRMTSSN SSSMLQDVEA GRRTEIEAIT
     GALIRMADRY EVAVPLHRMM YRLILASCE
//
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