ID Q5K9U0_CRYNJ Unreviewed; 605 AA.
AC Q5K9U0;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
GN OrderedLocusNames=CNK00780 {ECO:0000313|EMBL:AAW46124.1};
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW46124.1, ECO:0000313|Proteomes:UP000002149};
RN [1] {ECO:0000313|EMBL:AAW46124.1, ECO:0000313|Proteomes:UP000002149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- FUNCTION: Catalyzes oxidation of L-threonate to 2-oxo-tetronate. Can
CC use either NAD(+) or NADP(+) as cosubstrate, with a preference for
CC NAD(+). {ECO:0000256|ARBA:ARBA00037062}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonate + NAD(+) = 2-dehydro-L-erythronate + H(+) + NADH;
CC Xref=Rhea:RHEA:52548, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57561, ChEBI:CHEBI:57945, ChEBI:CHEBI:136669;
CC EC=1.1.1.411; Evidence={ECO:0000256|ARBA:ARBA00036958};
CC -!- SIMILARITY: Belongs to the HIBADH-related family. L-threonate
CC dehydrogenase subfamily. {ECO:0000256|ARBA:ARBA00037979}.
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DR EMBL; AE017351; AAW46124.1; -; Genomic_DNA.
DR RefSeq; XP_567641.1; XM_567641.1.
DR AlphaFoldDB; Q5K9U0; -.
DR STRING; 214684.Q5K9U0; -.
DR PaxDb; 214684-Q5K9U0; -.
DR EnsemblFungi; AAW46124; AAW46124; CNK00780.
DR GeneID; 3254696; -.
DR KEGG; cne:CNK00780; -.
DR VEuPathDB; FungiDB:CNK00780; -.
DR eggNOG; KOG0409; Eukaryota.
DR HOGENOM; CLU_021873_0_0_1; -.
DR InParanoid; Q5K9U0; -.
DR OMA; CINPAFS; -.
DR OrthoDB; 1121581at2759; -.
DR Proteomes; UP000002149; Chromosome 11.
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; 2.
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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43060:SF17; L-THREONATE DEHYDROGENASE; 1.
DR Pfam; PF14833; NAD_binding_11; 2.
DR Pfam; PF03446; NAD_binding_2; 2.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Reference proteome {ECO:0000313|Proteomes:UP000002149}.
FT DOMAIN 9..162
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 180..290
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 358..459
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 476..597
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
SQ SEQUENCE 605 AA; 63667 MW; 5269E783DB6AE915 CRC64;
MINEQKPVVG WIGLGAMGSG MAASLVSQGY KVQAFDVYPP SLKRVAEQGA IPSSSPRDAA
EGVQVLCLMV VNAQQVEETL FGKDGGVAEI LKNGASIIVF STVPPSFLVE VARRLDKLGK
NIGLVDSPVS GGSTRAAQGQ LAIMSSGTPS SIATARTVLD SLTLPPQGGL TLVGDRVGIA
SDFKMINQVF CAVSIAAQGE ALGLAKALGL NVRTVYEIVK QTTGDSFMFG HRAPWSIRPD
PIPKSAMTII NKDIAIVMGE ARRDHFPAPL SAAAEQLYTA ALAVGLEKEE DGLVSKFWEK
LGGEPIAEQG TEEEEIEKAR ELVIKPGKKV QKVLLATKNI DSRISYLKET LKKAGVEVVE
QGKEVDAVIV SAGSAAAVEE LLLHISSAGL SVNTPVIIIS NVLPSSRLSQ LAIEIKPLQL
IDAPTAGGSK EAKGGSLTVF ASGEADALSA SHSILSALSI QGGDSTKLHF IAGGVGSATK
VKAVNSLLEA IHLAVTGEGF AFAKHKGMDI EKVFKVLSGG AARSFIMGDR FPRIIKKSSQ
DAPENTVSTL WNDLSITLAE AKQHKCPFFL TQAAMQQLER LHSSGYADAD DSSIIKLWEE
TGVKI
//
