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Database: UniProt
Entry: A0A0U1Q3K8_9BURK
LinkDB: A0A0U1Q3K8_9BURK
Original site: A0A0U1Q3K8_9BURK 
ID   A0A0U1Q3K8_9BURK        Unreviewed;       358 AA.
AC   A0A0U1Q3K8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=AAV94_00170 {ECO:0000313|EMBL:KKW69339.1};
OS   Lampropedia cohaerens.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Lampropedia.
OX   NCBI_TaxID=1610491 {ECO:0000313|EMBL:KKW69339.1, ECO:0000313|Proteomes:UP000050580};
RN   [1] {ECO:0000313|EMBL:KKW69339.1, ECO:0000313|Proteomes:UP000050580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT6 {ECO:0000313|EMBL:KKW69339.1,
RC   ECO:0000313|Proteomes:UP000050580};
RA   Tripathi C., Rani P., Mahato N.K., Lal R.;
RT   "Draft genome sequence of Lampropedia sp. CT6, isolated from the microbial
RT   mat of a hot water spring, located at Manikaran, India.";
RL   Submitted (MAY-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:KKW69339.1}.
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DR   EMBL; LBNQ01000005; KKW69339.1; -; Genomic_DNA.
DR   RefSeq; WP_046740307.1; NZ_LBNQ01000005.1.
DR   AlphaFoldDB; A0A0U1Q3K8; -.
DR   STRING; 1610491.AAV94_00170; -.
DR   PATRIC; fig|1610491.3.peg.35; -.
DR   OrthoDB; 9796561at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000050580; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000050580}.
FT   DOMAIN          12..178
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          207..326
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          337..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   358 AA;  38287 MW;  970D7302CD338EFF CRC64;
     MNTRNVSSAL RVGIAGAGAI GCTLAALLAR AGARVHVLAR GASLTSLRSE GVRLHRRGDC
     LQAPVLASDD ASGLGPQDVL FLCAKAHDMQ QLLRSALPMI GPETCVVPLV NGVPWWYFQA
     LPGPWQGRRV QAVDPEGTLS ALLPATQIVG AVVFITAERV RPGEVVSDNP LLMVLGEIDH
     AGSSARLQRL ADWLERAGIE ARVTPQIRDA LWTKILANLT SNPLSVISGA TLQSIYGDTR
     LLAIVWEMLR EGLSLAAAFG ARIAFTPANF IREGAAMGAV RTSMLQDFEA GRRLELAAIG
     DAVLELATLQ DIAMPVTERV IALAHFRDEA RAASDDIAPV DPTQLPKPNK EVFHEQCR
//
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