TENAC_ARATH
ID TENAC_ARATH Reviewed; 617 AA.
AC F4KFT7; Q0WLK4; Q0WQD9;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Bifunctional TH2 protein, mitochondrial {ECO:0000303|PubMed:27677881};
DE AltName: Full=THIAMINE REQUIRING 2 {ECO:0000303|PubMed:27677881};
DE Includes:
DE RecName: Full=Thiamine phosphate phosphatase {ECO:0000303|PubMed:27677881};
DE EC=3.1.3.100 {ECO:0000269|PubMed:27677881};
DE Includes:
DE RecName: Full=Aminopyrimidine aminohydrolase {ECO:0000303|PubMed:25014715};
DE EC=3.5.99.2 {ECO:0000269|PubMed:27677881};
DE Flags: Precursor;
GN Name=TH2 {ECO:0000303|PubMed:27677881};
GN Synonyms=TH-2 {ECO:0000303|PubMed:27677881},
GN TNEA_C {ECO:0000303|PubMed:25014715};
GN OrderedLocusNames=At5g32470 {ECO:0000312|Araport:AT5G32470};
GN ORFNames=F18O9.80 {ECO:0000312|EMBL:AF296831};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
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, CATALYTIC ACTIVITY, MUTAGENESIS OF MET-47; CYS-213 AND ASP-317,
RP DOMAIN, BIOPHYSICOCHEMICAL PROPERTIES, ALTERNATIVE SPLICING, AND
RP SUBCELLULAR LOCATION.
RX PubMed=27677881; DOI=10.1105/tpc.16.00600;
RA Mimura M., Zallot R., Niehaus T.D., Hasnain G., Gidda S.K., Nguyen T.N.,
RA Anderson E.M., Mullen R.T., Brown G., Yakunin A.F., de Crecy-Lagard V.,
RA Gregory J.F., McCarty D.R., Hanson A.D.;
RT "Arabidopsis TH2 encodes the orphan enzyme thiamin monophosphate
RT phosphatase.";
RL Plant Cell 28:2683-2696(2016).
CC -!- FUNCTION: May be involved in the salvage of thiamine breakdown products
CC (PubMed:25014715). This protein has a haloacid dehalogenase family
CC domain fused to its TenA domain (PubMed:25014715). Phosphatase with the
CC highest activity against thiamine monophosphate (ThMP) and, with a
CC lower activity, against thiamine diphosphate (ThDP), flavin
CC mononucleotide, inorganic pyrophosphate, CTP and dATP
CC (PubMed:27677881). Has a thiamine salvage hydrolase activity, but only
CC against 4-amino-5-aminomethyl-2-methylpyrimidine (amino-HMP) and not
CC against N-formylamino-HMP, desthiothiamine, thiamine, ThMP, and ThDP
CC (PubMed:27677881). {ECO:0000269|PubMed:27677881,
CC ECO:0000305|PubMed:25014715}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + thiamine phosphate = phosphate + thiamine;
CC Xref=Rhea:RHEA:47948, ChEBI:CHEBI:15377, ChEBI:CHEBI:18385,
CC ChEBI:CHEBI:37575, ChEBI:CHEBI:43474; EC=3.1.3.100;
CC Evidence={ECO:0000269|PubMed:27677881};
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:27677881};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.86 uM for thiamine monophosphate {ECO:0000269|PubMed:27677881};
CC Note=kcat is 13.5 sec(-1) for thiamine monophosphate.
CC {ECO:0000269|PubMed:27677881};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC {ECO:0000269|PubMed:27677881}. Cytoplasm {ECO:0000269|PubMed:27677881}.
CC Note=Localized to the mitochondrion when the first start codon is
CC preceded by a strong Kozak sequence. {ECO:0000269|PubMed:27677881}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:27677881}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4KFT7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4KFT7-2; Sequence=VSP_058706;
CC -!- DOMAIN: The thiamine monophosphate phosphatase activity resides in the
CC HAD domain (297-571), while the TenA domain (85-292) has thiamine
CC salvage hydrolase activity (PubMed:27677881).
CC {ECO:0000269|PubMed:27677881}.
CC -!- MISCELLANEOUS: Knockdown mutants show reductions in root length and
CC shoot growth. {ECO:0000269|PubMed:27677881}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the TenA family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the HAD-like
CC hydrolase superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF00660.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF02003.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF296831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93884.1; -; Genomic_DNA.
DR EMBL; AK228760; BAF00660.1; ALT_INIT; mRNA.
DR EMBL; AK230194; BAF02003.1; ALT_INIT; mRNA.
DR RefSeq; NP_198287.3; NM_122826.5. [F4KFT7-1]
DR AlphaFoldDB; F4KFT7; -.
DR SMR; F4KFT7; -.
DR STRING; 3702.AT5G32470.1; -.
DR PaxDb; F4KFT7; -.
DR PRIDE; F4KFT7; -.
DR ProteomicsDB; 234255; -. [F4KFT7-1]
DR EnsemblPlants; AT5G32470.1; AT5G32470.1; AT5G32470. [F4KFT7-1]
DR GeneID; 833206; -.
DR Gramene; AT5G32470.1; AT5G32470.1; AT5G32470. [F4KFT7-1]
DR KEGG; ath:AT5G32470; -.
DR Araport; AT5G32470; -.
DR TAIR; locus:2145816; AT5G32470.
DR eggNOG; ENOG502QQU0; Eukaryota.
DR HOGENOM; CLU_035372_0_0_1; -.
DR InParanoid; F4KFT7; -.
DR OMA; GHINRQM; -.
DR PhylomeDB; F4KFT7; -.
DR BioCyc; ARA:AT5G32470-MON; -.
DR BioCyc; MetaCyc:GQT-4007-MON; -.
DR PRO; PR:F4KFT7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KFT7; baseline and differential.
DR Genevisible; F4KFT7; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0050334; F:thiaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0042131; F:thiamine phosphate phosphatase activity; IDA:TAIR.
DR GO; GO:0009228; P:thiamine biosynthetic process; IMP:TAIR.
DR Gene3D; 1.20.910.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR InterPro; IPR004305; Thiaminase-2/PQQC.
DR Pfam; PF03070; TENA_THI-4; 2.
DR SUPFAM; SSF48613; SSF48613; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Mitochondrion;
KW Multifunctional enzyme; Reference proteome; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..617
FT /note="Bifunctional TH2 protein, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432581"
FT ACT_SITE 213
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P25052"
FT ACT_SITE 286
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P25052"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P25052"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P25052"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P25052"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305|PubMed:27677881"
FT /id="VSP_058706"
FT MUTAGEN 47
FT /note="M->L: No effect on the mitochondrial localization."
FT /evidence="ECO:0000269|PubMed:27677881"
FT MUTAGEN 213
FT /note="C->A: Loss of hydrolase activity."
FT /evidence="ECO:0000269|PubMed:27677881"
FT MUTAGEN 317
FT /note="D->A: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:27677881"
FT CONFLICT 504
FT /note="E -> G (in Ref. 3; BAF02003)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 617 AA; 68964 MW; FB7C9F4EF9392354 CRC64;
MRFLFPTRLI NNSSLGLLRS PHTTAPIRSL WFRTKSPVFR SATTPIMTAV AFSSSLSIPP
TSEEALPGKL WIKFNRECLF SIYSPFAVCL AAGNLKIDTF RQYIAQDVHF LKAFAHAYEL
AADCADDDDD KLAISDLRKS VMEELKMHDS FVQDWDLDIN KEVSVNSATL RYTEFLLATA
SGKVEGCKAP GMLDTPFEKT KVAAYTLGAV TPCMRLYAFL GKEFGSLLDL SDVNHPYKKW
IDNYSSDAFQ ASAKQTEDLL EKLSVSMTGE ELDIIEKLYQ QAMKLEVEFF HAQPLAQPTI
VPLLKNHSKD DLVIFSDFDL TCTVVDSSAI LAEIAIVTAP KDEQSRSGQQ IHRMLSSDLK
NTWNLLSKQY TEHYEECIES ILNKKKADKF DYEGLCKALE QLSDFEKEAN NRVIESGVLK
GLNLEDIKRA GERLILQDGC INVFQKILKT ENLNAELHVL SYCWCGDLIR AAFSAGGVDA
VEVHANEFTF EESISTGEIE RKVESPINKA QQFKSILQNR KNENNKKSFL SVYIGDSVGD
LLCLLEADIG IVVSSSSSLR RVGSHFGVSF VPLFSGIVQK QKQHTEESSS SAWKGLSGTL
YTVSSWAEIH SFALGWE
