PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID 676765190
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Sisymbrieae; Sisymbrium
Family Trihelix
Protein Properties Length: 1036aa    MW: 115627 Da    PI: 7.8262
Description Trihelix family protein
Gene Model
Gene Model ID Type Source Coding Sequence
676765190genomeVEGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1trihelix735.2e-23724824186
   trihelix   1 rWtkqevlaLiearremeerlr....rgk...........lkkplWeevskkmrergferspkqCkekwenlnkrykkikegekkr.tsessstcpyfdq 84 
                +Wt+ +v++Li a+ +m+++ +                  +kk++W++vs++m e+gf++sp+qC++k+++lnkryk+++++ +++ +++++++  ++d+
  676765190 724 KWTDTMVRLLIMAVFYMGDEGGglglG-DqtegkkksgmlQKKGKWKSVSRAMVEKGFSVSPQQCEDKFNDLNKRYKRVNDILGRGtACRVVENQGLLDN 822
                7**************999999944430.134566788899**********************************************559******99999 PP

   trihelix  85 le 86 
                ++
  676765190 823 MD 824
                98 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SuperFamilySSF536863.01E-99116468IPR001926Tryptophan synthase beta subunit-like PLP-dependent enzyme
TIGRFAMsTIGR011242.4E-204116602IPR005787Threonine dehydratase, biosynthetic
CDDcd015622.62E-142118422No hitNo description
PfamPF002914.5E-80131416IPR001926Tryptophan synthase beta subunit-like PLP-dependent enzyme
PROSITE patternPS001650154167IPR000634Serine/threonine dehydratase, pyridoxal-phosphate-binding site
Gene3DG3DSA:3.40.50.11005.2E-38162258No hitNo description
Gene3DG3DSA:3.40.1020.106.6E-45325506No hitNo description
PfamPF005855.5E-20431520IPR001721ACT-like domain
CDDcd049062.46E-31440523No hitNo description
PROSITE profilePS5167211.002441512IPR001721ACT-like domain
Gene3DG3DSA:3.40.1020.107.0E-31507606No hitNo description
SuperFamilySSF550214.58E-21521606No hitNo description
PfamPF005851.5E-21527606IPR001721ACT-like domain
CDDcd049073.70E-33533601No hitNo description
PROSITE profilePS5167216.425534605IPR001721ACT-like domain
PfamPF138374.4E-20722850No hitNo description
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006520Biological Processcellular amino acid metabolic process
GO:0009097Biological Processisoleucine biosynthetic process
GO:0004794Molecular FunctionL-threonine ammonia-lyase activity
GO:0030170Molecular Functionpyridoxal phosphate binding
Sequence ? help Back to Top
Protein Sequence    Length: 1036 aa     Download sequence    Send to blast
MDSVRLPTAP SSLRSQMLGH PLPNRLHHIP LPPCNRHCNL RSKPAFGITR SRNHVSPMAV  60
ITGDEPSLAP TLTVDSPPPP RLKVSPNSLR YPAGYLGAVP ERTSDPENGS IAEAMEYLTN  120
ILSTKVYDIA IESPLHLAKK LSERLGVRMF LKREDLQPVF SFKLRGAYNM MAKLSGEQLA  180
KGVICSSAGN HAQGVALSAK KLGCTAVIVM PRTTPEIKWQ SVEDLGATVV LVGDSYDEAQ  240
AFAKQRAEEE GLTFIPPFDH PDIIAGQGTV GMEITRQAKG PIHAIFVPVG GGGLIAGIAA  300
YVKRVSPEVK IIGVEPADAN AMALSLHHGE RVILNQVGGF ADGVAVKEVG EETFRICKKL  360
LDGVVLVTRD AMCASIKDMF EEKRNILEPA GALSLAGAEA YCKYYGLKDV NVVVITSGAN  420
MNFDKLRIVT ELANVGRQQE AVLATLLPEK AGSFKQFCEL VGPMDITEFK YRCGSGQEAV  480
VLYSVGVHTP GELKELQKRM ESSQLRTRNL TTSDLVKDHL RYLMGGRSSV EDEVLCRFTF  540
PERPGALMNF LDSFSPRWNI SLFHYRAQGE AGANVLVGIQ VLEHEMEEFR NRAQDLGYEY  600
VLRQQDIVEE YSPKDSRLFF VFLLKKASVR KKELGMEPNV MFSGFSPRML SLEMPQNPPN  660
PVQFQHPHPM KYPYATKAKQ LSPISGGGGG DDEDRGSGSG SGCHPEDSAG TEGKRRVSQW  720
HRMKWTDTMV RLLIMAVFYM GDEGGGLGLG DQTEGKKKSG MLQKKGKWKS VSRAMVEKGF  780
SVSPQQCEDK FNDLNKRYKR VNDILGRGTA CRVVENQGLL DNMDHISPKL KDEVKKLLNS  840
KHLFFKEMCA YHNSCGHLDQ IPQPQQQPQS CFHAVESGKM ARIAESEEED ESDMVADDSD  900
SEMEDSEDEE EDTRKKRRRV EGVSAAVKRM REETTRVLED AGKSSWEKKE WMKRKALELE  960
ERKVGYEWEA VEMEKQRVKW IRYRSKKERE MDKAKLDNQR RSLETERMVL ILRRREIELT  1020
ELHLAGKRVD PSSATG
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
1tdj_A1e-1301045994498BIOSYNTHETIC THREONINE DEAMINASE
Search in ModeBase
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
1915919KRRRV
Functional Description ? help Back to Top
Source Description
UniProtCatalyzes the formation of alpha-ketobutyrate from threonine in a two-step reaction. The first step is a dehydration of threonine, followed by rehydration and liberation of ammonia.
Cis-element ? help Back to Top
SourceLink
PlantRegMap676765190
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankAF0962810.0AF096281.1 Arabidopsis thaliana threonine dehydratase/deaminase (OMR1) mRNA, complete cds.
GenBankAY0650370.0AY065037.1 Arabidopsis thaliana AT3g10050/T22K18_12 mRNA, complete cds.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_013583545.10.0PREDICTED: threonine dehydratase biosynthetic, chloroplastic-like
SwissprotQ9ZSS60.0THD1_ARATH; Threonine dehydratase biosynthetic, chloroplastic
TrEMBLA0A0D3CLJ20.0A0A0D3CLJ2_BRAOL; Threonine dehydratase
TrEMBLA0A3P6FR030.0A0A3P6FR03_BRAOL; Threonine dehydratase
STRINGBo5g137780.10.0(Brassica oleracea)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT3G10040.11e-168sequence-specific DNA binding transcription factors
Publications ? help Back to Top
  1. Mourad G,King J
    L-O-Methylthreonine-Resistant Mutant of Arabidopsis Defective in Isoleucine Feedback Regulation.
    Plant Physiol., 1995. 107(1): p. 43-52
    [PMID:12228340]
  2. Jander G, et al.
    Ethylmethanesulfonate saturation mutagenesis in Arabidopsis to determine frequency of herbicide resistance.
    Plant Physiol., 2003. 131(1): p. 139-46
    [PMID:12529522]
  3. Chivasa S, et al.
    Proteomic analysis of differentially expressed proteins in fungal elicitor-treated Arabidopsis cell cultures.
    J. Exp. Bot., 2006. 57(7): p. 1553-62
    [PMID:16547123]
  4. Joshi V,Laubengayer KM,Schauer N,Fernie AR,Jander G
    Two Arabidopsis threonine aldolases are nonredundant and compete with threonine deaminase for a common substrate pool.
    Plant Cell, 2006. 18(12): p. 3564-75
    [PMID:17172352]
  5. Less H,Galili G
    Principal transcriptional programs regulating plant amino acid metabolism in response to abiotic stresses.
    Plant Physiol., 2008. 147(1): p. 316-30
    [PMID:18375600]
  6. Joshi V,Jander G
    Arabidopsis methionine gamma-lyase is regulated according to isoleucine biosynthesis needs but plays a subordinate role to threonine deaminase.
    Plant Physiol., 2009. 151(1): p. 367-78
    [PMID:19571310]
  7. Yu H,Zhang F,Wang G,Liu Y,Liu D
    Partial deficiency of isoleucine impairs root development and alters transcript levels of the genes involved in branched-chain amino acid and glucosinolate metabolism in Arabidopsis.
    J. Exp. Bot., 2013. 64(2): p. 599-612
    [PMID:23230023]
  8. Xing A,Last RL
    A Regulatory Hierarchy of the Arabidopsis Branched-Chain Amino Acid Metabolic Network.
    Plant Cell, 2017. 29(6): p. 1480-1499
    [PMID:28522547]