ID A0A078G1M1_BRANA Unreviewed; 1382 AA.
AC A0A078G1M1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-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 Name=BnaC05g14020D {ECO:0000313|EMBL:CDY19201.1};
GN ORFNames=GSBRNA2T00006497001 {ECO:0000313|EMBL:CDY19201.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY19201.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY19201.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
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; LK032093; CDY19201.1; -; Genomic_DNA.
DR STRING; 3708.A0A078G1M1; -.
DR PaxDb; 3708-A0A078G1M1; -.
DR EnsemblPlants; CDY19201; CDY19201; GSBRNA2T00006497001.
DR Gramene; CDY19201; CDY19201; GSBRNA2T00006497001.
DR OMA; PIAVHYD; -.
DR Proteomes; UP000028999; Unassembled WGS sequence.
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; 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; 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.
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:UP000028999};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..166
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 173..288
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 327..485
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 492..612
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 659..901
FT /note="Four-carbon acid sugar kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07005"
FT DOMAIN 926..1092
FT /note="Four-carbon acid sugar kinase nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF17042"
SQ SEQUENCE 1382 AA; 148004 MW; 37E927AFC799885B CRC64;
MGGDGGAVVG FVGLDLFSFE LASSLLRSGF KVQAFEISTE MVEKFTELGG CKCDSPADVG
KGAAAVVVLL SHPDQIQDVI FGDEGVIKGI QKGAVLLLSS TIPPLHLQKL EKQITEGKEQ
IFVVDAYVLK GMSELLDGKL MIIASGRSDS ITRAQPYLTA MCQKLYTFEG EIGAGSKVKM
VNELLEGVHL VAAVEAISLG SQAGVHPWIL YDIISNAAGN SWIYKNHIPL LLKSDMDGHF
LDVLSQNLGI VEDKAKSLPF PVPLLAVARQ QLILGISQMH GDDTSISLAK IWEKVLGVGI
LEAANKELYK PEDLAKEITT QAKHVKRIGF IGLGAMGFGM AAHLLKSNFS VRGYDVYKPT
LVRFESVGGL AANSPADVTK DVDVLVIMVT NEVQAEDVLY GHLGAVEVIP SGTTVVLAST
VSPAFVSQLE RRLENEGKDL KLVDAPVSGG VKRAAMGELT IMASGTEDAL KSAGMVLSAL
SEKLYVIRGG CGAGSGVKMV NQLLAGVHIA SAAEAMAFGA RLGLNTRKLF NVISNCGGTS
WMFENRVPHM LDNDYTPYSA LDIFVKDLGI VTRDGSSRKV PLHISTVAHQ LFLAGSAAGW
GRIDDAGVVK VYETLGGVKV EGRLPVLKKQ DVLKSLPSEW PFDPTEDIHR LNMGKSKTLV
VLDDDPTGTQ TVHDVEVLTE WSVESISEQF RKKPVCFFIL TNSSSNCIFL KQASALIKDI
CTNLCAASKE SGNADYTIVL RGDSTLRGHF PQASLEADAA VSILGEMDAW IICPFFLQGG
RYTIDDVHYV ADSDRLVPAG ETEFAKDASF GYKSSNLREW VEEKTAGAVP ANSVESISIQ
LLRTGGPDAV CEFLCSLKKG SACIVNAASD RDMAVFAAGM IQAEQKGKSF LCRTAASFVS
ARIGIIPKDL VLPKDFASDK ESCGALIVVG SYVPKTTKQV EELQSQHKQK LRSIEISVEK
VALKSSEVRA AEISRAVEMA DAFLRAGRET LIMSSRELIT GKTSSESLDI NSKVSSALVE
VVSQITTRPR YILAKGGITS SDTATKALKA RRALVIGQAL AGVPVWKLGP ESRHPGVPYI
VFPGNVGSST ALAEVVKSWS VVAGRSTKEL LLNAENGGYA IGAFNVYNLE GIEAVVEAAE
EENSPAILQV HPGAFKQGGI PLVSCCISAA EQARVPMSVH FDHGTTKHEL LEALELGFDS
VMVDGSHLSF TENVSYTKTI TELARSKNIM VEAELGRLSG TEDGLTVEDY EAKLTNVHQA
QEFMETGIDA LAVCIGNVHG KYPESGPNLK LDLLKELHNL SSKKGVVLVL HGASGLPEKL
IKECIENGVR KFNVNTEVRK AYMDALTSEK KTDLVDLMSA TKTAMKAVIA DKIRLFGSAG
KA
//
