TENA2_MAIZE
ID TENA2_MAIZE Reviewed; 224 AA.
AC B6TPF2; B4FCM0;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Bifunctional TENA2 protein {ECO:0000303|PubMed:25136345};
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 {ECO:0000303|PubMed:18937034};
GN Name=TENA2 {ECO:0000303|PubMed:25136345};
GN Synonyms=pco111209, TENA_E {ECO:0000303|PubMed:25014715};
GN ORFNames=GRMZM2G080501 {ECO:0000305},
GN ZEAMMB73_374394 {ECO:0000312|EMBL:AFW88599.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DEVELOPMENTAL 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 [5]
RP FUNCTION.
RX PubMed=25136345; DOI=10.3389/fpls.2014.00370;
RA Guan J.C., Hasnain G., Garrett T.J., Chase C.D., Gregory J., Hanson A.D.,
RA McCarty D.R.;
RT "Divisions of labor in the thiamin biosynthetic pathway among organs of
RT maize.";
RL Front. Plant Sci. 5:370-370(2014).
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 ECO:0000305|PubMed:25136345}.
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 + thiamine = 4-amino-5-hydroxymethyl-2-methylpyrimidine +
CC 5-(2-hydroxyethyl)-4-methylthiazole + H(+); Xref=Rhea:RHEA:17509,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892,
CC ChEBI:CHEBI:17957, ChEBI:CHEBI:18385; EC=3.5.99.2;
CC Evidence={ECO:0000269|PubMed:25014715};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000305}.
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 -!- SIMILARITY: Belongs to the thiaminase-2 family. {ECO:0000305}.
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DR EMBL; CM000785; AFW88599.1; -; Genomic_DNA.
DR EMBL; EU966867; ACG38985.1; -; mRNA.
DR EMBL; BT034858; ACF79863.1; -; mRNA.
DR RefSeq; NP_001131451.1; NM_001137979.1.
DR AlphaFoldDB; B6TPF2; -.
DR SMR; B6TPF2; -.
DR STRING; 4577.GRMZM2G080501_P01; -.
DR PaxDb; B6TPF2; -.
DR EnsemblPlants; Zm00001eb396140_T001; Zm00001eb396140_P001; Zm00001eb396140.
DR EnsemblPlants; Zm00001eb396140_T002; Zm00001eb396140_P002; Zm00001eb396140.
DR GeneID; 100192786; -.
DR Gramene; Zm00001eb396140_T001; Zm00001eb396140_P001; Zm00001eb396140.
DR Gramene; Zm00001eb396140_T002; Zm00001eb396140_P002; Zm00001eb396140.
DR KEGG; zma:100192786; -.
DR MaizeGDB; 9025331; -.
DR eggNOG; ENOG502QQ9D; Eukaryota.
DR HOGENOM; CLU_055855_1_0_1; -.
DR OMA; FNTWLVQ; -.
DR OrthoDB; 1133952at2759; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000007305; Chromosome 9.
DR ExpressionAtlas; B6TPF2; baseline and differential.
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 Disulfide bond; Hydrolase; Reference proteome; Thiamine biosynthesis.
FT CHAIN 1..224
FT /note="Bifunctional TENA2 protein"
FT /id="PRO_0000432582"
FT ACT_SITE 213
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P25052"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ASY9"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ASY9"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ASY9"
FT DISULFID 153..168
FT /evidence="ECO:0000250|UniProtKB:Q9ASY9"
FT CONFLICT 152
FT /note="F -> L (in Ref. 3; ACF79863)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 25234 MW; 8E2BB2AB6F5A8D42 CRC64;
MDGGGVDTAT TAAWMEKHRH MYERATRHPF TVSIRDGTVD MSAFKRWLSQ DYLFVREFVA
FIASVLLKCC KQEDSSDMEI ILGGVASISD EISWFKNEAT VWGVDLASVS PLKANLEYHR
FLRSFTEPEI SYAVAVTTFW TIETVYQDSF GFCIQDGNKT PPELLGTCQR WGSAGFRQYC
QSLQSIVDRC LANAPADAVQ SAEEAFVRVL ELEIGFWDMS SSRS
