GenomeNet

Database: UniProt
Entry: A0A0F7KFQ0_9PROT
LinkDB: A0A0F7KFQ0_9PROT
Original site: A0A0F7KFQ0_9PROT 
ID   A0A0F7KFQ0_9PROT        Unreviewed;       344 AA.
AC   A0A0F7KFQ0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=AAW31_09330 {ECO:0000313|EMBL:AKH37973.1}, BCL69_11113
GN   {ECO:0000313|EMBL:TYP71582.1};
OS   Nitrosomonas communis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=44574 {ECO:0000313|EMBL:AKH37973.1, ECO:0000313|Proteomes:UP000034156};
RN   [1] {ECO:0000313|Proteomes:UP000034156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm2 {ECO:0000313|Proteomes:UP000034156};
RA   Kozlowski J.A., Kits K.D., Stein L.Y.;
RT   "Draft genome of Nitrosomonas communis strain Nm2.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AKH37973.1, ECO:0000313|Proteomes:UP000034156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm2 {ECO:0000313|EMBL:AKH37973.1,
RC   ECO:0000313|Proteomes:UP000034156};
RX   PubMed=26769932;
RA   Kozlowski J.A., Kits K.D., Stein L.Y.;
RT   "Genome Sequence of Nitrosomonas communis Strain Nm2, a Mesophilic Ammonia-
RT   Oxidizing Bacterium Isolated from Mediterranean Soil.";
RL   Genome Announc. 4:0-0(2016).
RN   [3] {ECO:0000313|EMBL:TYP71582.1, ECO:0000313|Proteomes:UP000324176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm2 {ECO:0000313|EMBL:TYP71582.1,
RC   ECO:0000313|Proteomes:UP000324176};
RA   Wagner M.;
RT   "Active sludge and wastewater microbial communities from Klosterneuburg,
RT   Austria.";
RL   Submitted (JUL-2019) 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   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP011451; AKH37973.1; -; Genomic_DNA.
DR   EMBL; VNHT01000111; TYP71582.1; -; Genomic_DNA.
DR   RefSeq; WP_046850041.1; NZ_VNHT01000111.1.
DR   AlphaFoldDB; A0A0F7KFQ0; -.
DR   KEGG; nco:AAW31_09330; -.
DR   PATRIC; fig|44574.3.peg.2280; -.
DR   OrthoDB; 8543548at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000034156; Chromosome.
DR   Proteomes; UP000324176; 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; 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   Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034156}.
FT   DOMAIN          8..143
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          176..312
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   344 AA;  37968 MW;  B5B7E72274BBFEA1 CRC64;
     MNLLNKPIHI LGAGGIGAAV GWALARAGYT VVLIDSHPNK ISEGKKNGVT VVGIGTQAVP
     FMAFDEWIAP NEGFILLCTK TYNNPEILTR LPEDAFLVPI QNGFDAALER RHHACEGIAS
     FVSECLRGRA ETRITRPGTL HIGARRSVTA WEWDEIASLA KALAKTKLFP VELVKDIQPY
     KATKLMYNAA ISPLAAVAGL DNGALLTDLL AKKLFFGMLY ENYAILKHAH IKLARIGPFH
     PDTVSYILRM TALSKLMAIF FRPSLRGTYC SMAPDISVDY CRTEIEAYNG YLIQLAGNFP
     CPLNRAVLAL FERIASENLK PHRKYLQYLV DSLPEGVLLD SSRR
//
DBGET integrated database retrieval system