ID A0A0D2SG52_GOSRA Unreviewed; 1373 AA.
AC A0A0D2SG52;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
GN ORFNames=B456_005G132300 {ECO:0000313|EMBL:KJB30170.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB30170.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB30170.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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; CM001744; KJB30170.1; -; Genomic_DNA.
DR RefSeq; XP_012478532.1; XM_012623078.1.
DR STRING; 29730.A0A0D2SG52; -.
DR EnsemblPlants; KJB30170; KJB30170; B456_005G132300.
DR GeneID; 105794087; -.
DR Gramene; KJB30170; KJB30170; B456_005G132300.
DR KEGG; gra:105794087; -.
DR eggNOG; KOG0409; Eukaryota.
DR eggNOG; KOG4153; Eukaryota.
DR OrthoDB; 1121581at2759; -.
DR Proteomes; UP000032304; Chromosome 5.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00947; TBP_aldolase_IIB; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
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; 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; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
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 NCBIfam; TIGR00167; cbbA; 1.
DR PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43060:SF17; L-THREONATE DEHYDROGENASE; 1.
DR Pfam; PF01116; F_bP_aldolase; 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; SSF51569; Aldolase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF142764; YgbK-like; 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:UP000032304};
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..281
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 322..480
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 487..607
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 654..891
FT /note="Four-carbon acid sugar kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07005"
FT DOMAIN 916..1082
FT /note="Four-carbon acid sugar kinase nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF17042"
SQ SEQUENCE 1373 AA; 147590 MW; C9EADB6F7C176EA5 CRC64;
MSGVIGFVGL DQLSLDMAAS LLRAGYKVQA FEVQNLLMNE FLKLGGTECF SLREAGKGVA
ALIVLISHVD QINDIIFGHD SALKGLQKDT VIILHSTILP SHIQKLEKNL REDGLTTSVV
DAYVFKATSE LLNGKIMVIS SGRSDAISKA YPFLSAMSEK LYTFEGETGA GSKTKLVTEL
LEGIHLIAAV EAISLGVKAG IHPWIIYDII SNAAGNSWVF KNYIPQLLSG NVKYNFLNPF
NHKLGIVLDM AKLLTFPLPL LASAHQQLAL GSLLGHGDDN TPLGQVWDQV FGVHTADAAN
AERYNPEELA TQITAKSKTV NRVGFIGLGA MGFGMATYLV KSNFCVVGYD VYKPTLTRFE
SAGGLIGSSP EDVSKGVDVL VVMVTNEAQA ESVLFGDLGA VSALPSGASI ILSSTVSPAY
VIQLERRLQN EGKDLKLVDA PVSGGVKRAS MGELTIMAAG SDDALKSAGL ILSALSEKLY
VIKGGCGAGS GVKMVNQLLA GVHIAASAEA MAFGARLGLS TRMLFDIISN SGATSWMFEN
RVPHMLDNDY TPYSALDIFV KDLGIVAREC SAHKIPLHIS TIAHQLFIAG SAAGWGRQDD
AGVVKVYETL TGVKVEGKLP ALKKEVVLQS LPPEWPVDPI NDIHKLNQKN SRTLVVLDDD
PTGTQTVHDV EVLTEWSIKS LVEQFRKKPI CFYILTNSRA LSSEKATVLI KDICNNLCSA
AKSVQHIDYT VVLRGDSTLR GHFPEEPDAA VSILGQVDAW ILCPFFLQGG RYTIDDIHYV
ADSDRLVPAG DTEFANDAAF GYKSSNLREW VEEKTAGRIP ASSVASISIQ LLRKGGPDAV
CELLCSLEKG STCIVNAVSE RDMAVFAAGM IQAELKGKSF LCRSAASFVS ARIGIISKAP
IRPKDLGISK ERSGGLIVVG SYVPKTTKQV EELHSQHGHM LKSLEVSVHK VAMKSSEERE
EEINRTAEMA SVFLAARKDT LIMSSRELIT GKTASESLEI NFKVSSALVE VVRRITTRPR
YILAKGGITS SDLATKALEA KRAKVVGQAL AGIPLWELGH ESRHPGVPYI VFPGNVGDSK
ALVEVVRSWA HPLRLSSTKE ILINAEKGSY AVGAFNVYNM EGVKAVVSAA EQERSPAILQ
VHPGAFKQGG VTLVACCISA AEEASVPITV HFDHGTSKQE LLESLELGFD SVMVDGSHLP
FKDNISYTKH ISNLAHLRDM LVEAELGRLS GTEDDLTVED YEAKLTDINQ AEEFIVETGI
DALAVCIGNV HGKYPASGPN LKLDLLKDLY ALSSKKGVFL VLHGASGLSK ELVKGCVERG
VRKFNVNTEV RKAYMESLSS PKGDLVHVMA STIEAMKAVV AEKMHLFGSA GKA
//
