ID A0A061FUZ4_THECC Unreviewed; 1024 AA.
AC A0A061FUZ4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
GN ORFNames=TCM_012876 {ECO:0000313|EMBL:EOY21355.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY21355.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY21355.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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}.
CC -!- SIMILARITY: Belongs to the four-carbon acid sugar kinase family.
CC {ECO:0000256|ARBA:ARBA00005715}.
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DR EMBL; CM001881; EOY21355.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FUZ4; -.
DR EnsemblPlants; EOY21355; EOY21355; TCM_012876.
DR Gramene; EOY21355; EOY21355; TCM_012876.
DR HOGENOM; CLU_002829_0_0_1; -.
DR Proteomes; UP000026915; Chromosome 3.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.980.20; Four-carbon acid sugar kinase, nucleotide binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.40.50.10840; Putative sugar-binding, N-terminal domain; 1.
DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR InterPro; IPR010737; 4-carb_acid_sugar_kinase_N.
DR InterPro; IPR037051; 4-carb_acid_sugar_kinase_N_sf.
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 InterPro; IPR031475; NBD_C.
DR InterPro; IPR042213; NBD_C_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 Pfam; PF17042; NBD_C; 1.
DR Pfam; PF07005; SBD_N; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF142764; YgbK-like; 1.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..162
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 169..285
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 322..472
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 473..539
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 586..823
FT /note="Four-carbon acid sugar kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07005"
FT DOMAIN 848..1008
FT /note="Four-carbon acid sugar kinase nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF17042"
SQ SEQUENCE 1024 AA; 110574 MW; 2ACF58A69C10A51A CRC64;
MAGVVGFVGL DRLSLDMAAL LLRAGYRVQA FEVQKLLMGE FLKLGGTECI SLMETGKGVA
ALIVLISHAD QINDVIFGHD DALKGLQKDK VIILHSTILP SYIQNLEKKL REDGLATSVV
DAYVYKATSD NLNGKVVVMS SGRSDAISKA RPFLSAMCEK LYIFEGETGA GSKIKLVTEL
LEGIHLMAAV EAISLGVHAG IHPWIIYDII SNAAGNSWVF KNYIPQLLRG SVKCHFLNPF
ILNLGIVLDM AKSLTFPLPL LATAHQQLVL GSSHGNGDDN TPLVQIWDQV YGVNTADAAN
TELYSPEQLA SQIIAKSKTV NRVGFIGLGA MGFGMATHLV KSNFCVLGYD VYRPTLIRFE
SAGGLIGTSP ADVSKDVDVL VVMVTNEAQA ESVLYGDLGA VSALPSGASI ILSSTVSPAF
VSQLERRLQN EGKDLKLVDA PVSGGVKRAS MGELTIMAAG SDDALKSSGL VLSVPHMLDN
DYTPYSALDI FVKDLGIVAR ECSTRKVPLH ISTMAHQLFL AGSAAGWGRQ DDAGVVKVYE
TLTGVKVEGK LPALKKEVVL QSIPPEWPVD PINDIHRLNQ KNSKTLVVLD DDPTGTQTVH
DVEVLTEWSV ESLVEQFRKK PICFFILTNS RSLSSEKATA LIKDICSSLL TAAKSVGNID
YTVVLRGDST LRGHFPEEPD AAVSVIGQVD AWILCPFFLQ GGRYTIEDIH YVADSDWLVP
AGDTEFAKDA AFGYKSSNLR EWVEEKTAGR IPASSVASIS IQLLRQGGPD AVCEHLCSLE
KGSTCIVNAV SERDMAVFAA GMIQAELKGK SFLCRSAASF VSARIGIIPK ARILPKDLGK
KKERSGGLIV VGSYVPKTTK QVEELQSQYG HMLKSIEVSV HKVAMKSLEE REEEINRTAE
MASVFLAAHK DTLIMSSREL ITGKTASESL EINFKVSSAL VEVVRRITTR PCYILAKGGI
TSSDLATKAL EAKRAKVVGQ ALAGIPLWEL GSESRHPGVP YIVFPGKFLV LFHLFQQILL
KAKL
//
