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Entry: A0A364K6T6_9BACL
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ID   A0A364K6T6_9BACL        Unreviewed;       318 AA.
AC   A0A364K6T6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
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=DL897_08040 {ECO:0000313|EMBL:RAL26003.1};
OS   Thermoflavimicrobium daqui.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Thermoflavimicrobium.
OX   NCBI_TaxID=2137476 {ECO:0000313|EMBL:RAL26003.1, ECO:0000313|Proteomes:UP000251213};
RN   [1] {ECO:0000313|EMBL:RAL26003.1, ECO:0000313|Proteomes:UP000251213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL26003.1,
RC   ECO:0000313|Proteomes:UP000251213};
RA   Wang X., Zhou H.;
RT   "Thermoflavimicrobium daqus sp. nov., a thermophilic microbe isolated from
RT   Moutai-flavour Daqu.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RAL26003.1, ECO:0000313|Proteomes:UP000251213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL26003.1,
RC   ECO:0000313|Proteomes:UP000251213};
RA   Zhirakovskaya E.;
RL   Submitted (JUN-2018) 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:RAL26003.1}.
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DR   EMBL; QJKK01000003; RAL26003.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A364K6T6; -.
DR   OrthoDB; 9800163at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000251213; 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|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:UP000251213}.
FT   DOMAIN          14..164
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          193..315
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   318 AA;  36408 MW;  89D896D3F4EC8EEF CRC64;
     MAPFLFGGDR MRTAVIGCGS LGLLWGARFT QIPGALTLLT RSKEQQQQLN QYGIDFESLD
     GRKKQIPVQA MWIEELPQPV QFDMVHVMVK QNHLPPIIPI LQEITSPTSR LLFWQNGLGH
     EKQIELLANR PWTYAAITTE GAHRSSYNTV KHTGKGETWV GPFPKLLTFD PPIQEWIIAV
     ENLGLQIAMD QQIFRRMWEK LAINCVVNPI TALHQVKNGE LLSSEYISEI EKISREVQAV
     AQKKGFSFEL DDMIQKVAYV CRNTKNNYSS MLQDLLQGRQ TEIDYMNGAI IRYGKEEKIP
     TAYNQYLVER IHHRENNG
//
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