TENAE_ARATH
ID TENAE_ARATH Reviewed; 221 AA.
AC Q9ASY9; Q8LBN8;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Bifunctional TENA-E protein {ECO:0000303|PubMed:25014715};
DE EC=3.5.1.- {ECO:0000305|PubMed:25014715};
DE EC=3.5.99.2 {ECO:0000269|PubMed:25014715};
DE AltName: Full=Aminopyrimidine aminohydrolase {ECO:0000303|PubMed:25014715};
DE AltName: Full=Formylaminopyrimidine amidohydrolase {ECO:0000303|PubMed:25014715};
DE AltName: Full=Formylaminopyrimidine deformylase {ECO:0000303|PubMed:25014715};
DE AltName: Full=Seed maturation protein PM36 homolog;
GN Name=TENA_E {ECO:0000303|PubMed:25014715};
GN OrderedLocusNames=At3g16990 {ECO:0000312|Araport:AT3G16990};
GN ORFNames=K14A17.22 {ECO:0000312|EMBL:AB026636}, K14A17_11;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, 3D-STRUCTURE MODELING, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=25014715; DOI=10.1042/bj20140522;
RA Zallot R., Yazdani M., Goyer A., Ziemak M.J., Guan J.C., McCarty D.R.,
RA de Crecy-Lagard V., Gerdes S., Garrett T.J., Benach J., Hunt J.F.,
RA Shintani D.K., Hanson A.D.;
RT "Salvage of the thiamin pyrimidine moiety by plant TenA proteins lacking an
RT active-site cysteine.";
RL Biochem. J. 463:145-155(2014).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 1-221 IN COMPLEX WITH HMP
RP (ISOFORM 1), AND DISULFIDE BOND.
RX PubMed=15326608; DOI=10.1002/prot.20213;
RA Blommel P.G., Smith D.W., Bingman C.A., Dyer D.H., Rayment I., Holden H.M.,
RA Fox B.G., Phillips G.N. Jr.;
RT "Crystal structure of gene locus At3g16990 from Arabidopsis thaliana.";
RL Proteins 57:221-222(2004).
CC -!- FUNCTION: Involved in thiamine salvage by hydrolyzing the thiamine
CC breakdown product 4-amino-5-aminomethyl-2-methylpyrimidine (amino-HMP)
CC to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) (PubMed:25014715).
CC Has a high formylamino-HMP amidohydrolase activity (PubMed:25014715).
CC No activity with other thiamine degradation products such as thiamine
CC mono- or diphosphate, oxothiamine, oxythiamine, thiamine disulfide,
CC desthiothiamine or thiochrome as substrates (PubMed:25014715). Does not
CC display thiaminase II activity, as it is unable to hydrolyze thiamine
CC (PubMed:25014715). Is able to carry out two successive steps in the
CC salvage of thiamine breakdown product, whereas two separate enzymes are
CC required in Bacillus species (Probable). May also serve a damage pre-
CC emption function by hydrolyzing products that would otherwise do harm
CC (Probable). {ECO:0000269|PubMed:25014715, ECO:0000305|PubMed:25014715}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-
CC hydroxymethyl-2-methylpyrimidine + NH4(+); Xref=Rhea:RHEA:31799,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16892, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:63416; EC=3.5.99.2;
CC Evidence={ECO:0000269|PubMed:25014715};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine = 4-
CC amino-5-aminomethyl-2-methylpyrimidine + formate;
CC Xref=Rhea:RHEA:46212, ChEBI:CHEBI:15377, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:63416, ChEBI:CHEBI:85895;
CC Evidence={ECO:0000269|PubMed:25014715};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=70 uM for N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine
CC {ECO:0000269|PubMed:25014715};
CC KM=1816 uM for 4-amino-5-aminomethyl-2-methylpyrimidine
CC {ECO:0000269|PubMed:25014715};
CC Note=kcat is 0.00281 sec(-1) for formylamino-HMP. kcat is 0.00015
CC sec(-1) for amino-HMP. {ECO:0000269|PubMed:25014715};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ASY9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ASY9-2; Sequence=VSP_013209;
CC -!- TISSUE SPECIFICITY: Expressed in roots and shoots.
CC {ECO:0000269|PubMed:25014715}.
CC -!- DEVELOPMENTAL STAGE: Expression increases during seed development.
CC {ECO:0000269|PubMed:25014715}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:25014715}.
CC -!- MISCELLANEOUS: [Isoform 1]: Used for 3D-structure determination.
CC -!- SIMILARITY: Belongs to the thiaminase-2 family. {ECO:0000305}.
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DR EMBL; AB026636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE75892.1; -; Genomic_DNA.
DR EMBL; AF361592; AAK32760.1; -; mRNA.
DR EMBL; AY058225; AAL15399.1; -; mRNA.
DR EMBL; AY087098; AAM64658.1; -; mRNA.
DR RefSeq; NP_188324.1; NM_112575.4. [Q9ASY9-1]
DR PDB; 2F2G; X-ray; 2.10 A; A/B=1-221.
DR PDB; 2Q4X; X-ray; 2.10 A; A/B=1-221.
DR PDBsum; 2F2G; -.
DR PDBsum; 2Q4X; -.
DR AlphaFoldDB; Q9ASY9; -.
DR SMR; Q9ASY9; -.
DR STRING; 3702.AT3G16990.1; -.
DR PaxDb; Q9ASY9; -.
DR PRIDE; Q9ASY9; -.
DR ProteomicsDB; 234256; -. [Q9ASY9-1]
DR EnsemblPlants; AT3G16990.1; AT3G16990.1; AT3G16990. [Q9ASY9-1]
DR GeneID; 820955; -.
DR Gramene; AT3G16990.1; AT3G16990.1; AT3G16990. [Q9ASY9-1]
DR KEGG; ath:AT3G16990; -.
DR Araport; AT3G16990; -.
DR TAIR; locus:2086052; AT3G16990.
DR eggNOG; ENOG502QQ9D; Eukaryota.
DR HOGENOM; CLU_055855_1_0_1; -.
DR InParanoid; Q9ASY9; -.
DR OMA; FNTWLVQ; -.
DR UniPathway; UPA00060; -.
DR EvolutionaryTrace; Q9ASY9; -.
DR PRO; PR:Q9ASY9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9ASY9; baseline and differential.
DR Genevisible; Q9ASY9; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050334; F:thiaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.910.10; -; 1.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR InterPro; IPR026285; TenA_E.
DR InterPro; IPR004305; Thiaminase-2/PQQC.
DR Pfam; PF03070; TENA_THI-4; 1.
DR PIRSF; PIRSF003170; Pet18p; 1.
DR SUPFAM; SSF48613; SSF48613; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Hydrolase;
KW Reference proteome; Thiamine biosynthesis.
FT CHAIN 1..221
FT /note="Bifunctional TENA-E protein"
FT /id="PRO_0000192044"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P25052"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15326608"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000303|PubMed:25014715"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000303|PubMed:25014715"
FT DISULFID 150..165
FT /evidence="ECO:0000269|PubMed:15326608"
FT VAR_SEQ 1..74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_013209"
FT CONFLICT 21
FT /note="A -> S (in Ref. 4; AAM64658)"
FT /evidence="ECO:0000305"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:2F2G"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:2F2G"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2F2G"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2F2G"
FT HELIX 38..67
FT /evidence="ECO:0007829|PDB:2F2G"
FT HELIX 74..98
FT /evidence="ECO:0007829|PDB:2F2G"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:2F2G"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:2F2G"
FT HELIX 129..146
FT /evidence="ECO:0007829|PDB:2F2G"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:2F2G"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:2F2G"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2F2G"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:2F2G"
FT HELIX 171..189
FT /evidence="ECO:0007829|PDB:2F2G"
FT HELIX 193..215
FT /evidence="ECO:0007829|PDB:2F2G"
SQ SEQUENCE 221 AA; 25070 MW; 9E5C7538FF04AFED CRC64;
MEKRGVIDTW IDKHRSIYTA ATRHAFVVSI RDGSVDLSSF RTWLGQDYLF VRRFVPFVAS
VLIRACKDSG ESSDMEVVLG GIASLNDEIE WFKREGSKWD VDFSTVVPQR ANQEYGRFLE
DLMSSEVKYP VIMTAFWAIE AVYQESFAHC LEDGNKTPVE LTGACHRWGN DGFKQYCSSV
KNIAERCLEN ASGEVLGEAE DVLVRVLELE VAFWEMSRGG Q
