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Database: UniProt
Entry: A0A1D3D0H7_9EIME
LinkDB: A0A1D3D0H7_9EIME
Original site: A0A1D3D0H7_9EIME 
ID   A0A1D3D0H7_9EIME        Unreviewed;       290 AA.
AC   A0A1D3D0H7;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Nad binding domain of 6-phosphogluconate {ECO:0000313|EMBL:OEH76909.1};
GN   ORFNames=cyc_08247 {ECO:0000313|EMBL:OEH76909.1};
OS   Cyclospora cayetanensis.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Cyclospora.
OX   NCBI_TaxID=88456 {ECO:0000313|EMBL:OEH76909.1, ECO:0000313|Proteomes:UP000095192};
RN   [1] {ECO:0000313|EMBL:OEH76909.1, ECO:0000313|Proteomes:UP000095192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHN_HEN01 {ECO:0000313|EMBL:OEH76909.1,
RC   ECO:0000313|Proteomes:UP000095192};
RX   PubMed=27129308; DOI=10.1186/s12864-016-2632-3;
RA   Liu S., Wang L., Zheng H., Xu Z., Roellig D.M., Li N., Frace M.A., Tang K.,
RA   Arrowood M.J., Moss D.M., Zhang L., Feng Y., Xiao L.;
RT   "Comparative genomics reveals Cyclospora cayetanensis possesses coccidia-
RT   like metabolism and invasion components but unique surface antigens.";
RL   BMC Genomics 17:316-316(2016).
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:OEH76909.1}.
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DR   EMBL; JROU02001282; OEH76909.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D3D0H7; -.
DR   VEuPathDB; ToxoDB:cyc_08247; -.
DR   VEuPathDB; ToxoDB:LOC34624016; -.
DR   InParanoid; A0A1D3D0H7; -.
DR   Proteomes; UP000095192; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR029154; HIBADH-like_NADP-bd.
DR   InterPro; IPR015815; HIBADH-related.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43060:SF15; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF14833; NAD_binding_11; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000103; HIBADH; 2.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095192}.
FT   DOMAIN          12..168
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          156..265
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   ACT_SITE        158
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ   SEQUENCE   290 AA;  30021 MW;  047A429327266C16 CRC64;
     MACIEATPGK ARIGWIGTGV MGVRMCENLL KKGFTLSVHT RTPSKAVPLQ QLGASVVSTA
     QEVAERSDIL CLMVGTPADV KKVLFGPQGA AIGLRSGCCL IDFTTSDPAL AEEVYVHLKS
     KGVHALDAPV SGGDIGARDG TLTVMAGGDP EALEAKTKLA NQITLCTNLV GLAEGLLYAE
     RAGLDLEKTL AVLMGGAATS WSVETYGPRV LAGNFNPGFA VAHLLKDLRL ALAEAARIKL
     ALPGLSLALQ LYEALEAQGG GVLGVHALKL ALQSLNSADQ RITDVAAQTQ
//
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