HINT3_ARATH
ID HINT3_ARATH Reviewed; 197 AA.
AC F4K1R2; Q8GWE2;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Adenylylsulfatase HINT3 {ECO:0000305};
DE EC=3.6.2.1 {ECO:0000269|PubMed:19896942};
DE AltName: Full=Histidine triad nucleotide-binding protein 3 {ECO:0000305};
GN Name=HINT3 {ECO:0000303|PubMed:19896942};
GN OrderedLocusNames=At5g48545 {ECO:0000312|Araport:AT5G48545};
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-112.
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=19329564; DOI=10.1104/pp.109.137703;
RA Reumann S., Quan S., Aung K., Yang P., Manandhar-Shrestha K., Holbrook D.,
RA Linka N., Switzenberg R., Wilkerson C.G., Weber A.P., Olsen L.J., Hu J.;
RT "In-depth proteome analysis of Arabidopsis leaf peroxisomes combined with
RT in vivo subcellular targeting verification indicates novel metabolic and
RT regulatory functions of peroxisomes.";
RL Plant Physiol. 150:125-143(2009).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19896942; DOI=10.1016/j.febslet.2009.11.003;
RA Guranowski A., Wojdyla A.M., Zimny J., Wypijewska A., Kowalska J.,
RA Jemielity J., Davis R.E., Bieganowski P.;
RT "Dual activity of certain HIT-proteins: A. thaliana Hint4 and C. elegans
RT DcpS act on adenosine 5'-phosphosulfate as hydrolases (forming AMP) and as
RT phosphorylases (forming ADP).";
RL FEBS Lett. 584:93-98(2010).
CC -!- FUNCTION: Possesses adenylylsulfatase activity in vitro.
CC {ECO:0000269|PubMed:19896942}.
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:19896942};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:19329564}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO50488.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAC43487.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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; AB020745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED95685.1; -; Genomic_DNA.
DR EMBL; AK118903; BAC43487.1; ALT_SEQ; mRNA.
DR EMBL; BT004955; AAO50488.1; ALT_SEQ; mRNA.
DR RefSeq; NP_974907.1; NM_203178.3.
DR AlphaFoldDB; F4K1R2; -.
DR SMR; F4K1R2; -.
DR STRING; 3702.AT5G48545.1; -.
DR iPTMnet; F4K1R2; -.
DR PaxDb; F4K1R2; -.
DR PRIDE; F4K1R2; -.
DR ProteomicsDB; 228802; -.
DR EnsemblPlants; AT5G48545.1; AT5G48545.1; AT5G48545.
DR GeneID; 2746201; -.
DR Gramene; AT5G48545.1; AT5G48545.1; AT5G48545.
DR KEGG; ath:AT5G48545; -.
DR Araport; AT5G48545; -.
DR TAIR; locus:1006230576; AT5G48545.
DR eggNOG; KOG3275; Eukaryota.
DR HOGENOM; CLU_056776_2_0_1; -.
DR InParanoid; F4K1R2; -.
DR OrthoDB; 1190598at2759; -.
DR PRO; PR:F4K1R2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K1R2; baseline and differential.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0047627; F:adenylylsulfatase activity; IDA:TAIR.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009150; P:purine ribonucleotide metabolic process; IDA:TAIR.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:TAIR.
DR CDD; cd01277; HINT_subgroup; 1.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR039384; HINT.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR001310; Histidine_triad_HIT.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR Pfam; PF01230; HIT; 1.
DR PRINTS; PR00332; HISTRIAD.
DR SUPFAM; SSF54197; SSF54197; 1.
DR PROSITE; PS00892; HIT_1; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Nucleotide-binding; Peroxisome; Reference proteome.
FT CHAIN 1..197
FT /note="Adenylylsulfatase HINT3"
FT /id="PRO_0000436747"
FT DOMAIN 51..158
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT REGION 14..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 143..147
FT /note="Histidine triad motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT COMPBIAS 25..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P49789"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P49789"
SQ SEQUENCE 197 AA; 21558 MW; 65ACC80BED9719F3 CRC64;
MEARRLAILC SHLNPPGPNP TRDPTLRVSD CSSGSSGDGK VESSTLQNDC VFCKIIRGES
PCLKLYEDDM CLCILDTNPL SHGHSLIIPK LHYPTLEETP PSVVAAMCSK VPLISNAIVK
ATGSDSFNLL VNNGAAAGQV IFHTHIHIIP RKERDCLWAS ESLRRHSLKL DKEASQLVSC
VRRHLCSLPE EQLVQPS
