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Database: UniProt
Entry: F2I7C0_AERUA
LinkDB: F2I7C0_AERUA
Original site: F2I7C0_AERUA 
ID   F2I7C0_AERUA            Unreviewed;       314 AA.
AC   F2I7C0; A0A9Q4H0Z2;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 56.
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   OrderedLocusNames=HMPREF9243_0432 {ECO:0000313|EMBL:AEA01776.1};
GN   ORFNames=ODY48_00830 {ECO:0000313|EMBL:MCY3054278.1};
OS   Aerococcus urinae (strain CCUG 59500 / ACS-120-V-Col10a).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus;
OC   Aerococcus incertae sedis.
OX   NCBI_TaxID=2976812 {ECO:0000313|EMBL:AEA01776.1, ECO:0000313|Proteomes:UP000008129};
RN   [1] {ECO:0000313|Proteomes:UP000008129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-120-V-Col10a {ECO:0000313|Proteomes:UP000008129};
RA   Durkin A.S., Madupu R., Radune D., Hostetler J., Torralba M., Gillis M.,
RA   Methe B., Sutton G., Nelson K.E.;
RT   "Complete genome sequence of Aerococcus urinae strain ACS-120-V-Col10a.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEA01776.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ACS-120-V-Col10a {ECO:0000313|EMBL:AEA01776.1};
RA   Durkin A.S., Madupu R., Radune D., Hostetler J., Torralba M., Gillis M.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:MCY3054278.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CDC-1656-U92 {ECO:0000313|EMBL:MCY3054278.1};
RA   Christensen J., Senneby E.;
RT   "Aerococcus urinae taxonomy study.";
RL   Submitted (SEP-2022) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP002512; AEA01776.1; -; Genomic_DNA.
DR   EMBL; JAOTMI010000002; MCY3054278.1; -; Genomic_DNA.
DR   RefSeq; WP_013669994.1; NC_015278.1.
DR   AlphaFoldDB; F2I7C0; -.
DR   STRING; 866775.HMPREF9243_0432; -.
DR   KEGG; aur:HMPREF9243_0432; -.
DR   PATRIC; fig|866775.3.peg.406; -.
DR   eggNOG; COG1893; Bacteria.
DR   HOGENOM; CLU_031468_0_0_9; -.
DR   OMA; NYSSMYQ; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000008129; Chromosome.
DR   Proteomes; UP001075187; Unassembled WGS sequence.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362068};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008129}.
FT   DOMAIN          3..149
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          185..308
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   314 AA;  34657 MW;  9EAC4737364FCD72 CRC64;
     MKIVILGAGG MGSRFGLMLK KAGKDVTLLD GWDKNIEAIR EHGIRANYNG EEVQVDIDIY
     PIDDFDPDLK ADLLIVFTKA MQLEDAIQAT RSIVTDQTKV LCLMNGIGYD DILRKYFDDE
     QIVLGNTMWT AGLEGPGRPK LFGNGYVNLL NLGKSEEAAA AAKDIVALLD EVGLNGVYEK
     EIFYLIYKKV CVNATMNGLC TILECNMADL GDAQASHDLI NQLVKEVVDV ANAEGVEMDL
     DEMIEHVGEC FNRETIGGHF PSMYQDLITN NRLTEIDYIN GAVAQKGEKL NVPTPYNQFL
     TSLVHTKEQL LGAK
//
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