ID H8GXX3_DEIGI Unreviewed; 318 AA.
AC H8GXX3;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Ketopantoate reductase ApbA/PanE {ECO:0000313|EMBL:AFD24705.1};
GN Name=apbA {ECO:0000313|EMBL:AFD24705.1};
GN OrderedLocusNames=DGo_CA0778 {ECO:0000313|EMBL:AFD24705.1};
OS Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD24705.1, ECO:0000313|Proteomes:UP000007575};
RN [1] {ECO:0000313|EMBL:AFD24705.1, ECO:0000313|Proteomes:UP000007575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC {ECO:0000313|Proteomes:UP000007575};
RX PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., Wang Y.,
RA Lin M.;
RT "Genome sequence and transcriptome analysis of the radioresistant bacterium
RT Deinococcus gobiensis: insights into the extreme environmental
RT adaptations.";
RL PLoS ONE 7:E34458-E34458(2012).
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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DR EMBL; CP002191; AFD24705.1; -; Genomic_DNA.
DR AlphaFoldDB; H8GXX3; -.
DR STRING; 745776.DGo_CA0778; -.
DR KEGG; dgo:DGo_CA0778; -.
DR PATRIC; fig|745776.4.peg.796; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_0_0_0; -.
DR Proteomes; UP000007575; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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;
FT DOMAIN 2..124
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 151..293
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 318 AA; 33956 MW; 28BBA13E12821F5B CRC64;
MTFVDQAADH VEAIRERGLS VTGPFGDFTV QAPAFTPGEV RGTWPLVLLC TKAQDTRAAA
GALAPHLDPD GVVVSVQNGL NTLTLDEVLG PERVLGSFVN FGADYLEPGV VLYGGRGAVV
VGEPSGGLSA RSAQVHALLR AFEPEAVHTP NIMGYLWSKL GYGALLFATA LTNDSIADAL
ARPEDRDTYT ELGREVMRVA LAHGVTPEAF NGFDPSAFLP QASRAQAQAS LDELVAFNRR
SAKTHSGIWR DLAVRRRRTE VDSQLGWVVH FGALHGVPTP LTTRLVALIH DIEEGRRPLD
RANLAELGQA RTPAGEGA
//
