PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
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(e.g., LFY)
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID KZV39672.1
Organism
Dorcoceras hygrometricum
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Lamiales; Gesneriaceae; Didymocarpoideae; Trichosporeae; Loxocarpinae; Dorcoceras
Family NAC
Protein Properties Length: 895aa    MW: 100589 Da    PI: 6.1316
Description NAC family protein
Gene Model
Gene Model ID Type Source Coding Sequence
KZV39672.1genomeCNUView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1NAM119.53.1e-37561803127
         NAM   3 pGfrFhPtdeelvveyLkkkvegkkleleevikevdiykvePwdLpkkvka.eekewyfFskrdkkyatgkrknratksgyWkatgkdkevlskkgelv 100
                 p frF+P++ el+v+ L kk++++  +  ++i++v++y + P++L +++k+ +e++wyfF+++++ky++g+r+ r++ +gyWkat  dk +++ ++e v
  KZV39672.1  56 PMFRFSPKETELIVDCLDKKINEEYAPYISIIPTVNVYLHTPNELAASYKSlGENDWYFFTSTERKYTNGSRPDRQAGNGYWKATVGDKMIYD-NHEFV 153
                 779**********************999999**************9655544889**************************************.999** PP

         NAM 101 glkktLvfykgrapkgektdWvmheyr 127
                 g+kk Lv+y+g++pkg+ktdW+m+e++
  KZV39672.1 154 GTKKCLVYYEGKHPKGKKTDWLMQEFK 180
                 **************************7 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SuperFamilySSF1019419.68E-4248206IPR003441NAC domain
PROSITE profilePS5100542.40854206IPR003441NAC domain
PfamPF023656.4E-1756180IPR003441NAC domain
Gene3DG3DSA:3.30.420.407.9E-7362391No hitNo description
PfamPF000127.7E-17363408IPR013126Heat shock protein 70 family
SuperFamilySSF530673.99E-11363408No hitNo description
PRINTSPR003016.4E-9364380IPR013126Heat shock protein 70 family
PRINTSPR003016.4E-9395415IPR013126Heat shock protein 70 family
SuperFamilySSF641531.7E-56439668IPR004443YjeF N-terminal domain
Gene3DG3DSA:3.40.50.102605.0E-67439671IPR004443YjeF N-terminal domain
HamapMF_0196619.645442677IPR004443YjeF N-terminal domain
TIGRFAMsTIGR001973.6E-41444639IPR004443YjeF N-terminal domain
PROSITE profilePS5138555.892446662IPR004443YjeF N-terminal domain
PfamPF038531.1E-32462634IPR004443YjeF N-terminal domain
TIGRFAMsTIGR005582.5E-86678895IPR000659Pyridoxamine 5'-phosphate oxidase
HamapMF_0162938.835688895IPR000659Pyridoxamine 5'-phosphate oxidase
SuperFamilySSF504751.22E-65692895IPR012349FMN-binding split barrel
Gene3DG3DSA:2.30.110.105.5E-83694895IPR012349FMN-binding split barrel
PfamPF012433.8E-28711797IPR011576Pyridoxamine 5'-phosphate oxidase-like, FMN-binding domain
PfamPF105901.3E-18851895IPR019576Pyridoxine 5'-phosphate oxidase, dimerisation, C-terminal
PROSITE patternPS010640861874IPR019740Pyridoxamine 5'-phosphate oxidase, conserved site
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0006734Biological ProcessNADH metabolic process
GO:0006739Biological ProcessNADP metabolic process
GO:0008615Biological Processpyridoxine biosynthetic process
GO:0042817Biological Processpyridoxal metabolic process
GO:0055114Biological Processoxidation-reduction process
GO:0005739Cellular Componentmitochondrion
GO:0005829Cellular Componentcytosol
GO:0009507Cellular Componentchloroplast
GO:0003677Molecular FunctionDNA binding
GO:0004733Molecular Functionpyridoxamine-phosphate oxidase activity
GO:0010181Molecular FunctionFMN binding
GO:0052856Molecular FunctionNADHX epimerase activity
GO:0052857Molecular FunctionNADPHX epimerase activity
Sequence ? help Back to Top
Protein Sequence    Length: 895 aa     Download sequence    Send to blast
MDSDQQSFMP VTPHRERASD ITSSILEEVS RGGDNQLITY HRRVSDGEYM AVHLSPMFRF  60
SPKETELIVD CLDKKINEEY APYISIIPTV NVYLHTPNEL AASYKSLGEN DWYFFTSTER  120
KYTNGSRPDR QAGNGYWKAT VGDKMIYDNH EFVGTKKCLV YYEGKHPKGK KTDWLMQEFK  180
SAKQSPRQPD GSMRLDNCVL CRIYKKSKHS SKRSQTPCCD SQDPRGISQS RRLCLGHTTN  240
QEELQTTYDS EYATNQQLIM QSPPQAAPQP TPWQNNFQLI LHPQQNLQSG VNDHDSHVFD  300
DLVDIETLSD FMSIDTVPNQ ALEHLDPQRF DSQHFELESA LAIDDHAFIL ELESLLAIDD  360
QAVIDEVIIV GSSTRIPAVQ ELVKKLTGKD PNVTVNPDEV VALGAALQQF RGYSFNSFTE  420
LKSMATATAR VVQDPESISY LNQREAAEID EILMGPLGFS VDQLMELAGL SVAASIAEVY  480
KPTECNRVLA ICGPGNNGGD GLVAARHLHH FGYKPVICYP KRTAKALYNG LVTQLESLSI  540
PFLLVEDLPV DLSTSYDVIV DAIFGFSFQG IPRPPFDGLI QRLADIGNLN QKQQKSPAIV  600
SVDIPSGWHV EEGDLSGKGI KPSMLVSLTA PKFCAKKFSG PHHFLGGRFV PPSIAEKFKL  660
NLPEYPGSSM CIRIGKPPRV DISTLRENYI SPEFSEDQAD ADPFAQFQKW FDDAMASGLK  720
EPNAMSLSTT GKDGKPSSRM VLLKGLDKDG FVWYTNYESQ KAHQISENPH AALLFYWDAL  780
NRQVRIEGPV QKVSDEESEK YFHSRPRGSQ IGAIVSKQST VISGRHILHQ QEKELEAQFA  840
DGSLIPKPKY WGGYRLKPQL FEFWQGQPSR LHDRLRYSPE VIARKNVWKI DRLSP
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
2dg2_A2e-7043767427258Apolipoprotein A-I binding protein
2dg2_B2e-7043767427258Apolipoprotein A-I binding protein
2dg2_C2e-7043767427258Apolipoprotein A-I binding protein
2dg2_D2e-7043767427258Apolipoprotein A-I binding protein
2dg2_E2e-7043767427258Apolipoprotein A-I binding protein
2dg2_F2e-7043767427258Apolipoprotein A-I binding protein
2o8n_A2e-7043767427258ApoA-I binding protein
3rno_A2e-7043767427258Apolipoprotein A-I-binding protein
3ro7_A2e-7043767427258Apolipoprotein A-I-binding protein
3roe_A2e-7043767427258Apolipoprotein A-I-binding protein
3roe_B2e-7043767427258Apolipoprotein A-I-binding protein
3roe_C2e-7043767427258Apolipoprotein A-I-binding protein
3roe_D2e-7043767427258Apolipoprotein A-I-binding protein
3roe_E2e-7043767427258Apolipoprotein A-I-binding protein
3roe_F2e-7043767427258Apolipoprotein A-I-binding protein
3rog_A2e-7043767427258Apolipoprotein A-I-binding protein
3rox_A2e-7043767427258Apolipoprotein A-I-binding protein
3roz_A2e-7043767427258Apolipoprotein A-I-binding protein
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtCatalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). Involved in the PLP salvage pathway. Has a higher preference for PNP over PMP. May also catalyze the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. {ECO:0000269|PubMed:17224143, ECO:0000269|PubMed:17873088}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapKZV39672.1
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: Circadian regulation. Up-regulated by light, heat, jasmonic acid, ethylene and abscisic acid treatments. Down-regulated by drought and salt treatment. Not induced by UV irradiation. {ECO:0000269|PubMed:21051239}.
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_011071781.20.0pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic isoform X1
RefseqXP_011071782.20.0pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic isoform X2
SwissprotQ9LTX30.0PPOX1_ARATH; Pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic
TrEMBLA0A2Z7BYF30.0A0A2Z7BYF3_9LAMI; NAD(P)H-hydrate epimerase
STRINGMigut.I00061.1.p0.0(Erythranthe guttata)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT1G69490.12e-41NAC-like, activated by AP3/PI
Publications ? help Back to Top
  1. Sang Y,Barbosa JM,Wu H,Locy RD,Singh NK
    Identification of a pyridoxine (pyridoxamine) 5'-phosphate oxidase from Arabidopsis thaliana.
    FEBS Lett., 2007. 581(3): p. 344-8
    [PMID:17224143]
  2. González E,Danehower D,Daub ME
    Vitamer levels, stress response, enzyme activity, and gene regulation of Arabidopsis lines mutant in the pyridoxine/pyridoxamine 5'-phosphate oxidase (PDX3) and the pyridoxal kinase (SOS4) genes involved in the vitamin B6 salvage pathway.
    Plant Physiol., 2007. 145(3): p. 985-96
    [PMID:17873088]
  3. Sang Y, et al.
    Expression, in vivo localization and phylogenetic analysis of a pyridoxine 5'-phosphate oxidase in Arabidopsis thaliana.
    Plant Physiol. Biochem., 2011. 49(1): p. 88-95
    [PMID:21051239]
  4. Herrero S,González E,Gillikin JW,Vélëz H,Daub ME
    Identification and characterization of a pyridoxal reductase involved in the vitamin B6 salvage pathway in Arabidopsis.
    Plant Mol. Biol., 2011. 76(1-2): p. 157-69
    [PMID:21533842]
  5. Niehaus TD, et al.
    Plants utilize a highly conserved system for repair of NADH and NADPH hydrates.
    Plant Physiol., 2014. 165(1): p. 52-61
    [PMID:24599492]
  6. Colinas M, et al.
    Balancing of B6 Vitamers Is Essential for Plant Development and Metabolism in Arabidopsis.
    Plant Cell, 2016. 28(2): p. 439-53
    [PMID:26858304]
  7. Colinas M,Fitzpatrick TB
    Interaction between vitamin B6 metabolism, nitrogen metabolism and autoimmunity.
    Plant Signal Behav, 2016. 11(4): p. e1161876
    [PMID:27018849]