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Database: UniProt
Entry: A0A0Q4GT23_9BURK
LinkDB: A0A0Q4GT23_9BURK
Original site: A0A0Q4GT23_9BURK 
ID   A0A0Q4GT23_9BURK        Unreviewed;       334 AA.
AC   A0A0Q4GT23;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=ASE76_07130 {ECO:0000313|EMBL:KQM75681.1};
OS   Xylophilus sp. Leaf220.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Xylophilus.
OX   NCBI_TaxID=1735686 {ECO:0000313|EMBL:KQM75681.1, ECO:0000313|Proteomes:UP000051325};
RN   [1] {ECO:0000313|EMBL:KQM75681.1, ECO:0000313|Proteomes:UP000051325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf220 {ECO:0000313|EMBL:KQM75681.1,
RC   ECO:0000313|Proteomes:UP000051325};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQM75681.1, ECO:0000313|Proteomes:UP000051325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf220 {ECO:0000313|EMBL:KQM75681.1,
RC   ECO:0000313|Proteomes:UP000051325};
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:KQM75681.1}.
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DR   EMBL; LMKO01000012; KQM75681.1; -; Genomic_DNA.
DR   RefSeq; WP_055839031.1; NZ_LMKO01000012.1.
DR   AlphaFoldDB; A0A0Q4GT23; -.
DR   STRING; 1735686.ASE76_07130; -.
DR   OrthoDB; 9796561at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000051325; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051325}.
FT   DOMAIN          3..105
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          196..315
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   334 AA;  34447 MW;  3D0DF5FC7A62F2B8 CRC64;
     MKVCIVGAGA IGGFIGARLA AAGQCDVSAL ARGATLAALQ AHGWRLQEGG ALLQRPARAE
     ADPQRLGLQD LVVIAVKGPA LSSLAPSLAP LIGPDTVLLP AMNGVPWWFC DRVPGWDGRP
     IESVDPGGRI AAALPAAQVL GCVVHASAST SAPGVVQHAM GQGLIVGEPA GGASARARRV
     ADLLAQAGFA ATVSADIRYD IWYKLWGNLT MNPLSAVTGA TMDRLLDDED LRGFCAQAMR
     ETAAVGAAID CSVAQTPEER FAVTRKLGAF RTSMLQDVEA GRPMELDAIV SAVQEIARRR
     GVATPAVDAL LGIARVFGQV HGLYPQNAKT PAAG
//
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