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Database: UniProt
Entry: A0A0D0S7I9_9FIRM
LinkDB: A0A0D0S7I9_9FIRM
Original site: A0A0D0S7I9_9FIRM 
ID   A0A0D0S7I9_9FIRM        Unreviewed;       397 AA.
AC   A0A0D0S7I9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=2-dehydropantoate 2-reductase {ECO:0000313|EMBL:KIR02137.1};
DE            EC=1.1.1.169 {ECO:0000313|EMBL:KIR02137.1};
GN   ORFNames=P261_00951 {ECO:0000313|EMBL:KIR02137.1};
OS   Lachnospiraceae bacterium TWA4.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1392836 {ECO:0000313|EMBL:KIR02137.1, ECO:0000313|Proteomes:UP000032079};
RN   [1] {ECO:0000313|EMBL:KIR02137.1, ECO:0000313|Proteomes:UP000032079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TWA4 {ECO:0000313|EMBL:KIR02137.1,
RC   ECO:0000313|Proteomes:UP000032079};
RX   PubMed=25495654;
RA   Gagen E.J., Wang J., Padmanabha J., Liu J., de Carvalho I., Liu J.,
RA   Webb R.I., Al Jassim R., Morrison M., Denman S.E., McSweeney C.S.;
RT   "Investigation of a new acetogen isolated from an enrichment of the tammar
RT   wallaby forestomach.";
RL   BMC Microbiol. 14:314-314(2014).
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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:KIR02137.1}.
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DR   EMBL; JPZU01000001; KIR02137.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0S7I9; -.
DR   STRING; 1392836.P261_00951; -.
DR   OrthoDB; 9772736at2; -.
DR   Proteomes; UP000032079; 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:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat 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   InterPro; IPR011990; TPR-like_helical_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   Oxidoreductase {ECO:0000313|EMBL:KIR02137.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032079}.
FT   DOMAIN          8..156
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          186..292
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   397 AA;  44482 MW;  5F7E23DAEB60387D CRC64;
     MDFNNSKIVV AGLGGVGGFL GAALASTYSN VIFYARGERK EALKNEGIYL TSEFIGDRHA
     TASLVTDNAE EIGIADILII SVKNYSLEEI CKQLQPVVDE HTLILPVLNG VDPADKTRSY
     FETGTVVDSL IYIISGSGPD FHITQSGPYA DLHIGNKTKD FKVNSAVHTI EDLFKPTGVK
     CIVEEDIEAA IWKKYIFNCA FNIMTAAHSA TVGELRENSE HVRDMRALLE EATSVAKAKK
     VNLPDDFVKE RMQFFKKKQA ASGTSSMKRD IDAGRPCELD TFSGYLLSEA LNFENLELPR
     TLHYYEILVK KIREATADSK LKELLDELNL AKETYGEKTI EVATCHYKLG MYYINHGNVS
     KAMEHLGDAL YIRRGFYKEE DIEIREIYYA LEQCTFM
//
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