GenomeNet

Database: UniProt
Entry: H3NY24_9GAMM
LinkDB: H3NY24_9GAMM
Original site: H3NY24_9GAMM 
ID   H3NY24_9GAMM            Unreviewed;       293 AA.
AC   H3NY24;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
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=OMB55_00004650 {ECO:0000313|EMBL:EHQ56748.1};
OS   gamma proteobacterium HIMB55.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX   NCBI_TaxID=745014 {ECO:0000313|EMBL:EHQ56748.1, ECO:0000313|Proteomes:UP000003408};
RN   [1] {ECO:0000313|EMBL:EHQ56748.1, ECO:0000313|Proteomes:UP000003408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HIMB55 {ECO:0000313|EMBL:EHQ56748.1,
RC   ECO:0000313|Proteomes:UP000003408};
RX   PubMed=22493201; DOI=10.1128/JB.00171-12;
RA   Huggett M.J., Rappe M.S.;
RT   "Genome Sequence of Strain HIMB55, a Novel Marine Gammaproteobacterium of
RT   the OM60/NOR5 Clade.";
RL   J. Bacteriol. 194:2393-2394(2012).
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:EHQ56748.1}.
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; AGIF02000001; EHQ56748.1; -; Genomic_DNA.
DR   AlphaFoldDB; H3NY24; -.
DR   STRING; 745014.OMB55_00004650; -.
DR   eggNOG; COG1893; Bacteria.
DR   OrthoDB; 6530772at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000003408; 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|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362068};
KW   Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW   ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003408}.
FT   DOMAIN          5..145
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          170..273
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   293 AA;  31711 MW;  21B2436B6DFF7C4B CRC64;
     MSDTWHILGV GSIGGLFAHR LHHGGATVRL LSRSTEASSR TIALKTAHST QSLSFNCSHV
     DEDGDISHLL ITSKSWAAGS ALREIRHRIG NHTTIVAMMN GMQHIDDIQM LAPECTLFLA
     TTTAGCHRAG EKWTAAGDGK TLIGRQDAGA APSWFGTWQK GIPSLEWCSD INERLVEKVA
     INACINPLTA VHGIKNGALL SERYKAKADQ IIAEVENILT ELGYAHLASR IEQTVRTVMA
     DTADNTSSML SDVMAGRRTE VDSIVGWLLD RSKGDHPELQ ALLSQLQSIE PTS
//
DBGET integrated database retrieval system