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Database: UniProt
Entry: G4Q5J0_ACIIR
LinkDB: G4Q5J0_ACIIR
Original site: G4Q5J0_ACIIR 
ID   G4Q5J0_ACIIR            Unreviewed;       324 AA.
AC   G4Q5J0;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
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   Name=apbA {ECO:0000313|EMBL:AEQ22093.1};
GN   OrderedLocusNames=Acin_0864 {ECO:0000313|EMBL:AEQ22093.1};
OS   Acidaminococcus intestini (strain RyC-MR95).
OC   Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC   Acidaminococcus.
OX   NCBI_TaxID=568816 {ECO:0000313|EMBL:AEQ22093.1, ECO:0000313|Proteomes:UP000007093};
RN   [1] {ECO:0000313|EMBL:AEQ22093.1, ECO:0000313|Proteomes:UP000007093}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RyC-MR95 {ECO:0000313|EMBL:AEQ22093.1,
RC   ECO:0000313|Proteomes:UP000007093};
RX   PubMed=22123762; DOI=10.1128/JB.06301-11;
RA   D'Auria G., Galan J.C., Rodriguez-Alcayna M., Moya A., Baquero F.,
RA   Latorre A.;
RT   "Complete genome sequence of Acidaminococcus intestini RYC-MR95, a Gram-
RT   negative bacterium from the phylum Firmicutes.";
RL   J. Bacteriol. 193:7008-7009(2011).
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; CP003058; AEQ22093.1; -; Genomic_DNA.
DR   RefSeq; WP_009014802.1; NC_016077.1.
DR   AlphaFoldDB; G4Q5J0; -.
DR   STRING; 568816.Acin_0864; -.
DR   GeneID; 72310299; -.
DR   KEGG; ain:Acin_0864; -.
DR   PATRIC; fig|568816.4.peg.835; -.
DR   eggNOG; COG1893; Bacteria.
DR   HOGENOM; CLU_031468_6_0_9; -.
DR   InParanoid; G4Q5J0; -.
DR   OMA; FKLWGNM; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000007093; 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   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007093}.
FT   DOMAIN          6..131
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          186..314
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   324 AA;  35361 MW;  69EBB38398C112B3 CRC64;
     MEIKKVALIG AGAIGSYLIW GLSRLADLSF TVIADGQRGE RLREKGLVIN GEPFRPMVQG
     AEETGPVDVI FVTVKYGALS AILPAVTALT DSRTMIISLM NGVDSEAVLE AAVGKGHIVP
     ALLRIASHRE RGKEGIDQVT FKEPQGIRGL YYGKPAPLSQ RDEVQLEALK AFFARTPLLT
     HMSRTIESDI WAKFLFNIGQ NIPQAIVGCG TGAYADSEHV RFLKERLEEE VVLVAKAKGI
     SLHTAILEPG KNGKGAGYTK SESPAVRHST LQDLDHHRHT EIDMLCGRMV EMGEALGIPT
     PYNAFAYHVI KALEEKNDGL FDYE
//
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