FHIT_ARATH
ID FHIT_ARATH Reviewed; 180 AA.
AC F4KEV7; Q84WL2; Q9LVM4;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Bifunctional bis(5'-adenosyl)-triphosphatase/adenylylsulfatase FHIT {ECO:0000305|PubMed:18694747};
DE EC=3.6.1.29 {ECO:0000269|PubMed:18694747};
DE AltName: Full=Adenosine 5'-monophosphoramidase FHIT {ECO:0000305|PubMed:18694747};
DE EC=3.9.1.- {ECO:0000269|PubMed:18694747};
DE AltName: Full=Adenylylsulfatase;
DE EC=3.6.2.1 {ECO:0000269|PubMed:18694747};
DE AltName: Full=Adenylylsulfate-ammonia adenylyltransferase;
DE EC=2.7.7.51 {ECO:0000269|PubMed:26181368};
DE AltName: Full=Fragile histidine triad protein {ECO:0000303|PubMed:18694747};
GN Name=FHIT {ECO:0000303|PubMed:18694747};
GN OrderedLocusNames=At5g58240 {ECO:0000312|Araport:AT5G58240};
GN ORFNames=MCK7.11 {ECO:0000312|EMBL:BAA96915.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18694747; DOI=10.1016/j.febslet.2008.07.060;
RA Guranowski A., Wojdyla A.M., Pietrowska-Borek M., Bieganowski P.,
RA Khurs E.N., Cliff M.J., Blackburn G.M., Blaziak D., Stec W.J.;
RT "Fhit proteins can also recognize substrates other than dinucleoside
RT polyphosphates.";
RL FEBS Lett. 582:3152-3158(2008).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26181368; DOI=10.1042/bsr20150135;
RA Wojdyla-Mamon A.M., Guranowski A.;
RT "Adenylylsulfate-ammonia adenylyltransferase activity is another inherent
RT property of Fhit proteins.";
RL Biosci. Rep. 35:0-0(2015).
CC -!- FUNCTION: Possesses dinucleoside triphosphate hydrolase activity
CC (PubMed:18694747). Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate
CC (Ap3A) to yield AMP and ADP (PubMed:18694747). Exhibits
CC adenylylsulfatase activity, hydrolyzing adenosine 5'-phosphosulfate to
CC yield AMP and sulfate (PubMed:18694747). Exhibits adenosine 5'-
CC monophosphoramidase activity, hydrolyzing purine nucleotide
CC phosphoramidates with a single phosphate group such as adenosine
CC 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2 (PubMed:18694747).
CC Exhibits adenylylsulfate-ammonia adenylyltransferase, catalyzing the
CC ammonolysis of adenosine 5'-phosphosulfate resulting in the formation
CC of adenosine 5'-phosphoramidate (PubMed:26181368).
CC {ECO:0000269|PubMed:18694747, ECO:0000269|PubMed:26181368}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(3)-bis(5'-adenosyl) triphosphate = ADP + AMP + 2
CC H(+); Xref=Rhea:RHEA:13893, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58529, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=3.6.1.29; Evidence={ECO:0000269|PubMed:18694747};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphosulfate + H2O = AMP + 2 H(+) + sulfate;
CC Xref=Rhea:RHEA:17041, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:58243, ChEBI:CHEBI:456215; EC=3.6.2.1;
CC Evidence={ECO:0000269|PubMed:18694747};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphosulfate + NH4(+) = adenosine 5'-
CC phosphoramidate + 2 H(+) + sulfate; Xref=Rhea:RHEA:19197,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57890, ChEBI:CHEBI:58243; EC=2.7.7.51;
CC Evidence={ECO:0000269|PubMed:26181368};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphoramidate + H2O = AMP + NH4(+);
CC Xref=Rhea:RHEA:67916, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57890, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:18694747};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for adenosine 5'-phosphoramidate (at pH 6.8)
CC {ECO:0000269|PubMed:18694747};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4KEV7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4KEV7-2; Sequence=VSP_058413;
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DR EMBL; AB019228; BAA96915.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97022.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97023.1; -; Genomic_DNA.
DR EMBL; BT003103; AAO24535.1; -; mRNA.
DR EMBL; AK228164; BAF00120.1; -; mRNA.
DR RefSeq; NP_200632.2; NM_125209.3. [F4KEV7-1]
DR RefSeq; NP_974957.1; NM_203228.2. [F4KEV7-2]
DR AlphaFoldDB; F4KEV7; -.
DR SMR; F4KEV7; -.
DR IntAct; F4KEV7; 1.
DR STRING; 3702.AT5G58240.1; -.
DR MetOSite; F4KEV7; -.
DR PaxDb; F4KEV7; -.
DR PRIDE; F4KEV7; -.
DR ProteomicsDB; 230078; -. [F4KEV7-1]
DR EnsemblPlants; AT5G58240.1; AT5G58240.1; AT5G58240. [F4KEV7-1]
DR EnsemblPlants; AT5G58240.2; AT5G58240.2; AT5G58240. [F4KEV7-2]
DR GeneID; 835936; -.
DR Gramene; AT5G58240.1; AT5G58240.1; AT5G58240. [F4KEV7-1]
DR Gramene; AT5G58240.2; AT5G58240.2; AT5G58240. [F4KEV7-2]
DR KEGG; ath:AT5G58240; -.
DR Araport; AT5G58240; -.
DR TAIR; locus:2161313; AT5G58240.
DR eggNOG; KOG3379; Eukaryota.
DR OMA; DAIYGMM; -.
DR BRENDA; 3.6.1.29; 399.
DR SABIO-RK; F4KEV7; -.
DR PRO; PR:F4KEV7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KEV7; baseline and differential.
DR GO; GO:0043530; F:adenosine 5'-monophosphoramidase activity; IDA:TAIR.
DR GO; GO:0047627; F:adenylylsulfatase activity; IDA:TAIR.
DR GO; GO:0047352; F:adenylylsulfate-ammonia adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047710; F:bis(5'-adenosyl)-triphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR CDD; cd01275; FHIT; 1.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR039383; FHIT.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR Pfam; PF01230; HIT; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
DR PROSITE; PS00892; HIT_1; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..180
FT /note="Bifunctional bis(5'-adenosyl)-
FT triphosphatase/adenylylsulfatase FHIT"
FT /id="PRO_0000436745"
FT DOMAIN 27..134
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT MOTIF 119..123
FT /note="Histidine triad motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT ACT_SITE 121
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P49789"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P49789"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P49789"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P49789"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform 2)"
FT /id="VSP_058413"
FT CONFLICT 59
FT /note="A -> G (in Ref. 3; AAO24535 and 4; BAF00120)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 20400 MW; 8C88EDB0E9D923FE CRC64;
MLNLQVTGKT ILSSIRCQRK MSSTCSSYAF GPYKIDPREV FYATPLSYAM VNLRPLLPAH
VLVCPRRLVP RFTDLTADET SDLWLTAQKV GSKLETFHNA SSLTLAIQDG PQAGQTVPHV
HIHILPRKGG DFEKNDEIYD ALDEKEKELK QKLDLDKDRV DRSIQEMADE ASQYRSLFDC
