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Database: UniProt
Entry: A0A0T2YG70_9BURK
LinkDB: A0A0T2YG70_9BURK
Original site: A0A0T2YG70_9BURK 
ID   A0A0T2YG70_9BURK        Unreviewed;       334 AA.
AC   A0A0T2YG70;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
DE            EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN   ORFNames=ASE11_14050 {ECO:0000313|EMBL:KRB97934.1};
OS   Hydrogenophaga sp. Root209.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1736490 {ECO:0000313|EMBL:KRB97934.1, ECO:0000313|Proteomes:UP000050889};
RN   [1] {ECO:0000313|Proteomes:UP000050889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root209 {ECO:0000313|Proteomes:UP000050889};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB97934.1, ECO:0000313|Proteomes:UP000050889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root209 {ECO:0000313|EMBL:KRB97934.1,
RC   ECO:0000313|Proteomes:UP000050889};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004994}.
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:KRB97934.1}.
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DR   EMBL; LMIE01000031; KRB97934.1; -; Genomic_DNA.
DR   RefSeq; WP_056275943.1; NZ_LMIE01000031.1.
DR   AlphaFoldDB; A0A0T2YG70; -.
DR   STRING; 1736490.ASE11_14050; -.
DR   OrthoDB; 9796561at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000050889; 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; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR21708:SF42; 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   4: Predicted;
FT   DOMAIN          11..113
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          206..322
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   334 AA;  34779 MW;  D84CBAD4480038EA CRC64;
     MTIATAHPRR IGIVGAGAIG GHLAARLAGA GHDVTLLARG ATLEALRTHG LRYTTGGQPE
     QRIAVRAESA PQAMGPQDLV VLALKSQALP TVVPTLQPLL ATDTPVLTLN NGLPWWYFLV
     PGQPLEGQRL SRVDPQGETE RAVELSRVLG GTIMASCYCP QPGVVVHSAG ARLAIGEPAG
     GVSERASLWS GVLAEAGLGA VASAQIRSDI WLKLLGNVCA NPLSLLTGAT TDRMLDDAGV
     SALFAAMMEE CIALGRRLGL TLETTTGQRM AQTRQLGAIR SSMLQDLEAG RSVELDAILG
     AAIECAQAVG QPVPRLQDVF ALACLRARSA GLYP
//
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