TTM1_ARATH
ID TTM1_ARATH Reviewed; 643 AA.
AC Q9C9B9;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Inorganic pyrophosphatase TTM1 {ECO:0000305};
DE EC=3.6.1.1 {ECO:0000269|PubMed:28733390};
DE AltName: Full=Triphosphate tunnel metalloenzyme 1 {ECO:0000303|PubMed:25185123};
DE Short=AtTTM1 {ECO:0000303|PubMed:25185123};
DE Flags: Precursor;
GN Name=TTM1 {ECO:0000303|PubMed:25185123};
GN OrderedLocusNames=At1g73980 {ECO:0000312|Araport:AT1G73980};
GN ORFNames=F2P9.15 {ECO:0000312|EMBL:AAG52525.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=25185123; DOI=10.1104/pp.114.248757;
RA Ung H., Moeder W., Yoshioka K.;
RT "Arabidopsis triphosphate tunnel metalloenzyme2 is a negative regulator of
RT the salicylic acid-mediated feedback amplification loop for defense
RT responses.";
RL Plant Physiol. 166:1009-1021(2014).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY LEAF SENESCENCE, SUBCELLULAR
RP LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, TISSUE SPECIFICITY, AND
RP CATALYTIC ACTIVITY.
RX PubMed=28733390; DOI=10.1104/pp.17.00700;
RA Ung H., Karia P., Ebine K., Ueda T., Yoshioka K., Moeder W.;
RT "Triphosphate tunnel metalloenzyme function in senescence highlights a
RT biological diversification of this protein superfamily.";
RL Plant Physiol. 175:473-485(2017).
CC -!- FUNCTION: Exhibits pyrophosphatase activity with stronger affinity for
CC pyrophosphate (PPi), moderate affinity for ATP and ADP, and weak
CC affinity for tripolyphosphate (PPPi). No activity observed toward
CC uridine substrate. Regulates positively natural and dark-induced leaf
CC senescence. {ECO:0000269|PubMed:28733390}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474; EC=3.6.1.1;
CC Evidence={ECO:0000269|PubMed:28733390};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:28733390};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16.7 uM for pyrophosphate {ECO:0000269|PubMed:28733390};
CC Vmax=284 nmol/min/ug enzyme with pyrophosphate as substrate
CC {ECO:0000269|PubMed:28733390};
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:28733390};
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:28733390}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues, with strong
CC expression detected in senescent leaves. {ECO:0000269|PubMed:28733390}.
CC -!- INDUCTION: Accumulates during leaf senescence.
CC {ECO:0000269|PubMed:28733390}.
CC -!- DISRUPTION PHENOTYPE: Delayed dark-induced and natural senescence.
CC {ECO:0000269|PubMed:28733390}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC016662; AAG52525.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35534.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58436.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58437.1; -; Genomic_DNA.
DR EMBL; AF462846; AAL58933.1; -; mRNA.
DR EMBL; BT002630; AAO11546.1; -; mRNA.
DR PIR; E96767; E96767.
DR RefSeq; NP_001320870.1; NM_001334620.1.
DR RefSeq; NP_001320871.1; NM_001334621.1.
DR RefSeq; NP_177538.1; NM_106057.3.
DR PDB; 7Z66; X-ray; 2.70 A; AAAA=20-412.
DR PDB; 7Z67; X-ray; 2.65 A; A=20-412.
DR PDBsum; 7Z66; -.
DR PDBsum; 7Z67; -.
DR AlphaFoldDB; Q9C9B9; -.
DR SMR; Q9C9B9; -.
DR STRING; 3702.AT1G73980.1; -.
DR iPTMnet; Q9C9B9; -.
DR PaxDb; Q9C9B9; -.
DR PRIDE; Q9C9B9; -.
DR ProteomicsDB; 234629; -.
DR EnsemblPlants; AT1G73980.1; AT1G73980.1; AT1G73980.
DR EnsemblPlants; AT1G73980.2; AT1G73980.2; AT1G73980.
DR EnsemblPlants; AT1G73980.3; AT1G73980.3; AT1G73980.
DR GeneID; 843736; -.
DR Gramene; AT1G73980.1; AT1G73980.1; AT1G73980.
DR Gramene; AT1G73980.2; AT1G73980.2; AT1G73980.
DR Gramene; AT1G73980.3; AT1G73980.3; AT1G73980.
DR KEGG; ath:AT1G73980; -.
DR Araport; AT1G73980; -.
DR TAIR; locus:2031541; AT1G73980.
DR eggNOG; KOG4203; Eukaryota.
DR HOGENOM; CLU_028566_0_0_1; -.
DR InParanoid; Q9C9B9; -.
DR OMA; AYIPRTY; -.
DR OrthoDB; 295827at2759; -.
DR PhylomeDB; Q9C9B9; -.
DR BioCyc; ARA:AT1G73980-MON; -.
DR PRO; PR:Q9C9B9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9B9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0016462; F:pyrophosphatase activity; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:1900055; P:regulation of leaf senescence; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR033469; CYTH-like_dom_sf.
DR InterPro; IPR023577; CYTH_domain.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006083; PRK/URK.
DR Pfam; PF01928; CYTH; 1.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55154; SSF55154; 1.
DR PROSITE; PS51707; CYTH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Plant defense; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..15
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 16..643
FT /note="Inorganic pyrophosphatase TTM1"
FT /id="PRO_0000444983"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 248..410
FT /note="CYTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01044"
SQ SEQUENCE 643 AA; 72408 MW; C1C96B8C970271D8 CRC64;
MALDSSVALS PRRRHGLLRD QVQLIKRKDS GRYEIVPIED PLSFEKGFYA VIRACQLLAQ
KNDGLILVGL AGPSGAGKTI FTEKILNFMP SIAIINMDNY NDGTRVIDGN FDDPRLTDYD
TLLDNIHGLR DGKPVQVPIY DFKSSSRIGY RTLEVPSSRI VILEGIYALS EKLRPLLDLR
VSVTGGVHFD LVKRVLRDIQ RAGQEPEEII HQISETVYPM YKAFIEPDLK TAQIKILNKF
NPFSGFQNPT YILKSSKAVT PEQMKAALSE DFKERTEETY DIYLLPPGED PEACQSYLRM
RNRDGKYNLM FEEWVTDRPF IISPRITFEV SVRLLGGLMA LGYTIATILK RKSHIFDDDK
VIVKTDWLEQ LNRTYVQVQG KDRTFVKNVA DQLGLEGSYV PHTYIEQIQL ERLVNDVLAL
PDDLKTKLSL DDDTVSSPKE ALSRASVDSR MKYLHGGVSK SYTNPRHKVL PNLTRLAVNN
RMLDARAPAS PATLPNQGFI TQLSDQISTL NERMDEFTSR IEELNSKIPN RIAPSGSQHN
LALPIENGNG SVLSFSASAS QLVRESPLME EVVLVARGQR QIMHQMDTLS NLLREYVGEK
TRIERLDSSR TNSTTQNLES STVPILLGLA IGCVGIFAYS RLK
