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Database: UniProt
Entry: A0A0L6U1V6_9FIRM
LinkDB: A0A0L6U1V6_9FIRM
Original site: A0A0L6U1V6_9FIRM 
ID   A0A0L6U1V6_9FIRM        Unreviewed;       303 AA.
AC   A0A0L6U1V6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=AKG39_07395 {ECO:0000313|EMBL:KNZ42327.1};
OS   Acetobacterium bakii.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Acetobacterium.
OX   NCBI_TaxID=52689 {ECO:0000313|EMBL:KNZ42327.1, ECO:0000313|Proteomes:UP000036873};
RN   [1] {ECO:0000313|Proteomes:UP000036873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8239 {ECO:0000313|Proteomes:UP000036873};
RA   Song Y., Hwang S., Cho B.-K.;
RT   "Draft genome sequence of Acetobacterium bakii DSM 8293, a potential
RT   psychrophilic chemical producer through syngas fermentation.";
RL   Submitted (JUL-2015) 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:KNZ42327.1}.
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DR   EMBL; LGYO01000016; KNZ42327.1; -; Genomic_DNA.
DR   RefSeq; WP_050739743.1; NZ_UOGO01000001.1.
DR   AlphaFoldDB; A0A0L6U1V6; -.
DR   STRING; 52689.AKG39_07395; -.
DR   PATRIC; fig|52689.4.peg.594; -.
DR   OrthoDB; 9793586at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000036873; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036873}.
FT   DOMAIN          7..148
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          177..300
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   303 AA;  33629 MW;  266E15C1520BE8BE CRC64;
     MTIKDVSIIG LGALGILFGH QISQKIGFDF SVIADQSRIE KYQSQGVFCN GEVCDFNYQS
     SEDGSIADLI IFAVKIDGLE AAIEAVKNHV GPETIFMSLL NGITSETIIG EAFGEVNLVW
     SVAQGMDTVK EGNQLFYTNP GIICFGNRNG DEPSEKVDRV REFFDRVGIA YEIDNRMDRK
     IWAKFMLNVG INQVVSVFGE NFGSVQLPGK PRELMIAAMN EVIPVARKEG VELTQADITY
     WLRVVDGLSP EGKPSMRQDV EARRPTEVEL FSGTVNRLGE KHGLETPVNE FLYDKIKTLE
     STF
//
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