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Database: UniProt
Entry: W3AR76_9FIRM
LinkDB: W3AR76_9FIRM
Original site: W3AR76_9FIRM 
ID   W3AR76_9FIRM            Unreviewed;       318 AA.
AC   W3AR76;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|RuleBase:RU362068};
DE            EC=1.1.1.169 {ECO:0000256|RuleBase:RU362068};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|RuleBase:RU362068};
GN   ORFNames=UYO_0433 {ECO:0000313|EMBL:ETP73496.1};
OS   Lachnospiraceae bacterium JC7.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1165092 {ECO:0000313|EMBL:ETP73496.1, ECO:0000313|Proteomes:UP000018967};
RN   [1] {ECO:0000313|EMBL:ETP73496.1, ECO:0000313|Proteomes:UP000018967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC7 {ECO:0000313|EMBL:ETP73496.1,
RC   ECO:0000313|Proteomes:UP000018967};
RA   Rosewarne C.P., Cheung J.L., Evans P.N., Tomkins N.W., Denman S.E.,
RA   O Cuiv P., Morrison M.;
RT   "Isolation and genomic characterisation of Lachnospiraceae sp. JC7, a newly
RT   identified member of the bovine rumen core microbiota.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC       pantoic acid. {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|RuleBase:RU362068};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {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:ETP73496.1}.
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DR   EMBL; ALYD01000003; ETP73496.1; -; Genomic_DNA.
DR   AlphaFoldDB; W3AR76; -.
DR   PATRIC; fig|1165092.3.peg.434; -.
DR   OrthoDB; 9772736at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000018967; 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; PTHR21708:SF26; 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   3: Inferred from homology;
KW   NADP {ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068}.
FT   DOMAIN          6..154
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          185..306
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   318 AA;  35669 MW;  A58C7337B5FA8A30 CRC64;
     MKNLKITVAG VGAIGGLLAA MLGRKYEESI TLVARGDHGK ALREKGLTLK SDFYGDSTMK
     PAAVAERGED IPVQDLVLIC CKNYSLDQLC EQIRPCIGAE TIVMPVMNGV EPGDRIREKF
     PEAVCIDSLI YTITAKDSDH SARQSGAYTH MFIGSKLRDE RHVEASKKVY ELFKEVGFDA
     RYTDDIMSEI WQKFILNCGF NVITARYLTN TGGVRGNEEW TKDFHKLMHE AEAVGLREGV
     NIPEGTAEKK FRYCMDNQSD DATSSLKRDV EAKRQAELDA FLGAVIRKAG KYGIDVPCSR
     RYYKELSEMI DSYMTQER
//
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