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Database: UniProt
Entry: A0A075LIQ4_9BACI
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ID   A0A075LIQ4_9BACI        Unreviewed;       293 AA.
AC   A0A075LIQ4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=GZ22_06335 {ECO:0000313|EMBL:AIF66274.1};
OS   Terribacillus goriensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Terribacillus.
OX   NCBI_TaxID=386490 {ECO:0000313|EMBL:AIF66274.1, ECO:0000313|Proteomes:UP000027980};
RN   [1] {ECO:0000313|EMBL:AIF66274.1, ECO:0000313|Proteomes:UP000027980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP602 {ECO:0000313|EMBL:AIF66274.1,
RC   ECO:0000313|Proteomes:UP000027980};
RA   Wang Y., Lu P., Zhang L.;
RT   "Complete genome sequence of a moderately halophilic bacterium
RT   Terribacillus aidingensis MP602, isolated from Cryptomeria fortunei in
RT   Tianmu mountain in China.";
RL   Submitted (JUL-2014) 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}.
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DR   EMBL; CP008876; AIF66274.1; -; Genomic_DNA.
DR   RefSeq; WP_038559921.1; NZ_CP008876.1.
DR   AlphaFoldDB; A0A075LIQ4; -.
DR   KEGG; tap:GZ22_06335; -.
DR   HOGENOM; CLU_031468_0_1_9; -.
DR   OrthoDB; 9800163at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000027980; Chromosome.
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|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362068};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027980}.
FT   DOMAIN          3..145
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          176..279
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   293 AA;  32852 MW;  77BBFC31EC9F0A18 CRC64;
     MKINVIGGGA IGLLAAAKLG RFHDVRLLTR TREQSDEITV KGLHLGDEVI TVEALPAADW
     QDLGQPDVWI VCVKQYDLQA IWEKLKLHAN AAVVFLQNGM NHTDFLQEED FNYPIIVGSV
     EHGALRINSH TVEHTGEAAI RLADLSDHYA KVLVNQLNKP DFPILFEQNW HMMLGTKLIA
     NAVINPLTAI YRVKNGELLE HPAFERIAKV LCKEAADALG LEGVQQWANV RRIINATKAN
     LSSMHRDIQA GRQTEIESIS GYVRDHAKQA VPYTDFVYYS ILGLTKQQER TYL
//
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