ID Q4UGE1_THEAN Unreviewed; 443 AA.
AC Q4UGE1;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating) {ECO:0000256|ARBA:ARBA00013011};
DE EC=1.1.1.44 {ECO:0000256|ARBA:ARBA00013011};
GN ORFNames=TA19350 {ECO:0000313|EMBL:CAI73848.1};
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874 {ECO:0000313|EMBL:CAI73848.1, ECO:0000313|Proteomes:UP000001950};
RN [1] {ECO:0000313|EMBL:CAI73848.1, ECO:0000313|Proteomes:UP000001950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ankara {ECO:0000313|Proteomes:UP000001950};
RX PubMed=15994557; DOI=10.1126/science.1110418;
RA Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA Shiels B., Tait A., Barrell B.G., Hall N.;
RT "Genome of the host-cell transforming parasite Theileria annulata compared
RT with T. parva.";
RL Science 309:131-133(2005).
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 3/3. {ECO:0000256|ARBA:ARBA00004874}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419}.
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DR EMBL; CR940347; CAI73848.1; -; Genomic_DNA.
DR RefSeq; XP_954525.1; XM_949432.1.
DR AlphaFoldDB; Q4UGE1; -.
DR STRING; 5874.Q4UGE1; -.
DR GeneID; 3864491; -.
DR KEGG; tan:TA19350; -.
DR VEuPathDB; PiroplasmaDB:TA19350; -.
DR eggNOG; KOG2653; Eukaryota.
DR InParanoid; Q4UGE1; -.
DR OMA; CVTHVGP; -.
DR OrthoDB; 3013545at2759; -.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000001950; Chromosome 1 part 1.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; 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; IPR006114; 6PGDH_C.
DR InterPro; IPR006113; 6PGDH_Gnd/GntZ.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006183; Pgluconate_DH.
DR PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1.
DR Pfam; PF00393; 6PGD; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000109; 6PGD; 1.
DR PRINTS; PR00076; 6PGDHDRGNASE.
DR SMART; SM01350; 6PGD; 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 Gluconate utilization {ECO:0000256|ARBA:ARBA00023064};
KW Oxidoreductase {ECO:0000313|EMBL:CAI73848.1};
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126};
KW Reference proteome {ECO:0000313|Proteomes:UP000001950}.
FT DOMAIN 188..441
FT /note="6-phosphogluconate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01350"
FT ACT_SITE 192
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT ACT_SITE 199
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
SQ SEQUENCE 443 AA; 50711 MW; 19781BC28B2BF9A2 CRC64;
MEDSKESEFG IVGLGVMASA YATNLYFRGF KVSVWTRSQK EIEIFNEKLK EQPKFNGLDA
DSVDLTRVKC YMNLEEFVLS LNRPRMILIL IIAGEAVDCV LDKLIPLLDR DDLVVDGGNE
WYNNTERRIL RCKEEGIRYS GMGISGGERG ALTHPCLMFG GNFEDYNKLK RIMSQADTDF
YVGPGSSGHY VKMVHNGIEY ALMQVISELY KLMKFENFMS NLEISSVFNS WHSQNYSYLL
QITQMILQVK EGEEHLLDKI MPCVSSNGTG KWTVQDSFDR GVPVPSIAIS VDMRSFSNLS
HHSNTNNTVK TSERSEKYKI DELKITYMCT LISIFSQGFH LISEASREFG WDLNLCKLAN
IWSRNAIISC DLLNEISKSF KENDQMLPFH PKFNGVLRDN MNVWKKVVKM CLENDIPVPG
IGNSLQYIQI LFNKHVNKIF YLI
//
