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Database: UniProt
Entry: G5IE26_9CLOT
LinkDB: G5IE26_9CLOT
Original site: G5IE26_9CLOT 
ID   G5IE26_9CLOT            Unreviewed;       307 AA.
AC   G5IE26;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=HMPREF9473_01753 {ECO:0000313|EMBL:EHI60262.1};
OS   Hungatella hathewayi WAL-18680.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX   NCBI_TaxID=742737 {ECO:0000313|EMBL:EHI60262.1, ECO:0000313|Proteomes:UP000005384};
RN   [1] {ECO:0000313|EMBL:EHI60262.1, ECO:0000313|Proteomes:UP000005384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAL-18680 {ECO:0000313|EMBL:EHI60262.1,
RC   ECO:0000313|Proteomes:UP000005384};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., Summanen P.H.,
RA   Molitoris D.R., Song M., Daigneault M., Allen-Vercoe E., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Clostridium hathewayi WAL-18680.";
RL   Submitted (AUG-2011) 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:EHI60262.1}.
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DR   EMBL; ADLN01000029; EHI60262.1; -; Genomic_DNA.
DR   RefSeq; WP_006779736.1; NZ_JH379027.1.
DR   AlphaFoldDB; G5IE26; -.
DR   PATRIC; fig|742737.3.peg.1778; -.
DR   HOGENOM; CLU_031468_0_0_9; -.
DR   OrthoDB; 9793586at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000005384; 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:UP000005384}.
FT   DOMAIN          3..149
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          176..300
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   307 AA;  32794 MW;  0445944137351D7C CRC64;
     MKIAIIGAGA MGSIYGGHLS LHNEVYLVDT NQSVVDQINE SGLRLLENGQ DVMYHPTAVT
     STEGLGEMDL VILFVKALFS KAALSANRGI IGPDTYVLTL QNGSGHEDIL SEFVDQEHII
     IGTTEDNGAV LEAGYVRHGG EGKTNVGMLT EDKNGMLPAV KASFDCCGFQ VRIHENIQEL
     IWDKLMTNVS LSAVTGVLQV KMGYIAANPY AWNLTSQLVK EAVAVAGGLG LTFDEEEVLE
     KVRTTSRNNP EGITSICADI VAGRKTEVDT ISGSVVRAAQ KSGVSAPTHE MIVNIIHALE
     GKETKTP
//
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