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Database: UniProt
Entry: A0A140DT98_9FIRM
LinkDB: A0A140DT98_9FIRM
Original site: A0A140DT98_9FIRM 
ID   A0A140DT98_9FIRM        Unreviewed;       322 AA.
AC   A0A140DT98;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=AALO17_07410 {ECO:0000313|EMBL:AMK53875.1};
OS   Faecalibaculum rodentium.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Faecalibaculum.
OX   NCBI_TaxID=1702221 {ECO:0000313|EMBL:AMK53875.1, ECO:0000313|Proteomes:UP000069771};
RN   [1] {ECO:0000313|EMBL:AMK53875.1, ECO:0000313|Proteomes:UP000069771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alo17 {ECO:0000313|EMBL:AMK53875.1,
RC   ECO:0000313|Proteomes:UP000069771};
RX   PubMed=26877770; DOI=10.1186/s13099-016-0087-3;
RA   Lim S., Chang D.H., Ahn S., Kim B.C.;
RT   "Whole genome sequencing of "Faecalibaculum rodentium" ALO17, isolated from
RT   C57BL/6J laboratory mouse feces.";
RL   Gut Pathog. 8:3-3(2016).
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}.
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DR   EMBL; CP011391; AMK53875.1; -; Genomic_DNA.
DR   RefSeq; WP_067555577.1; NZ_CP011391.1.
DR   AlphaFoldDB; A0A140DT98; -.
DR   STRING; 1702221.AALO17_07410; -.
DR   GeneID; 78477548; -.
DR   KEGG; fro:AALO17_07410; -.
DR   OrthoDB; 9793586at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000069771; Chromosome.
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   ECO:0000313|EMBL:AMK53875.1};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000069771}.
FT   DOMAIN          12..157
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          191..311
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   322 AA;  35083 MW;  D1E4E6446D675866 CRC64;
     MTAKTDSPIQ TVGIAGRGAI GLLYGMQMRS GGVEPWYIAD EERIWRYRQD PVPVNGIPQT
     FRYLQPGTTG NESAGDSHAG PALDLVLIMT KASGLEGALE EIAPFVDDHT IILSCLNGIT
     SEEIARERYP GNTILRTIVQ GMDTVYLHGE CHYSHIGEIL TGSDGPGQET AVRQVKAFFD
     SIGMPCRICE DIVREQWNKL MLNCGVNQIC AVYGCGYAGA VGEHRELFVR VMEEVRQVAL
     ARGIHLGTED IDRWLTVCEA LDGASMPSMA QDIRAGRHTE LCLFSGTVVP MAGILGIPVP
     ELSRLQDQIL ALEAGMEQPS RP
//
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