HINT1_ARATH
ID HINT1_ARATH Reviewed; 147 AA.
AC Q8GUN2; Q9LXZ1;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Adenylylsulfatase HINT1 {ECO:0000305};
DE EC=3.6.2.1 {ECO:0000269|PubMed:19896942};
DE AltName: Full=HIS triad family protein 3 {ECO:0000305};
DE AltName: Full=Histidine triad nucleotide-binding protein 1 {ECO:0000305};
GN Name=HINT1 {ECO:0000303|PubMed:19896942}; Synonyms=HIT3 {ECO:0000305};
GN OrderedLocusNames=At3g56490 {ECO:0000312|Araport:AT3G56490};
GN ORFNames=5P19_140 {ECO:0000312|EMBL:CAB88052.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
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 Plastid, chloroplast {ECO:0000269|PubMed:19329564}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM63920.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB88052.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AL163972; CAB88052.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE79527.1; -; Genomic_DNA.
DR EMBL; AY045861; AAK76535.1; -; mRNA.
DR EMBL; BT002356; AAN86189.1; -; mRNA.
DR EMBL; AY086874; AAM63920.1; ALT_INIT; mRNA.
DR PIR; T49050; T49050.
DR RefSeq; NP_567038.1; NM_115507.4.
DR AlphaFoldDB; Q8GUN2; -.
DR SMR; Q8GUN2; -.
DR IntAct; Q8GUN2; 1.
DR STRING; 3702.AT3G56490.1; -.
DR iPTMnet; Q8GUN2; -.
DR PaxDb; Q8GUN2; -.
DR PRIDE; Q8GUN2; -.
DR ProMEX; Q8GUN2; -.
DR ProteomicsDB; 230188; -.
DR EnsemblPlants; AT3G56490.1; AT3G56490.1; AT3G56490.
DR GeneID; 824816; -.
DR Gramene; AT3G56490.1; AT3G56490.1; AT3G56490.
DR KEGG; ath:AT3G56490; -.
DR Araport; AT3G56490; -.
DR TAIR; locus:2102554; AT3G56490.
DR eggNOG; KOG3275; Eukaryota.
DR HOGENOM; CLU_056776_8_0_1; -.
DR InParanoid; Q8GUN2; -.
DR OMA; SDCLFCK; -.
DR OrthoDB; 1190598at2759; -.
DR PhylomeDB; Q8GUN2; -.
DR BioCyc; ARA:AT3G56490-MON; -.
DR PRO; PR:Q8GUN2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8GUN2; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0047627; F:adenylylsulfatase activity; IDA:TAIR.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
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 Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR001310; Histidine_triad_HIT.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR PANTHER; PTHR23089; PTHR23089; 1.
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 Chloroplast; Hydrolase; Nucleotide-binding; Peroxisome; Plastid;
KW Reference proteome.
FT CHAIN 1..147
FT /note="Adenylylsulfatase HINT1"
FT /id="PRO_0000436746"
FT DOMAIN 37..147
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT MOTIF 131..135
FT /note="Histidine triad motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT ACT_SITE 133
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P49789"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P49789"
SQ SEQUENCE 147 AA; 16000 MW; 2BCFBE84D78F8B0D CRC64;
MSHRVSILSS HFSPASAVMA SEKEAALAAT PSDSPTIFDK IISKEIPSTV VFEDDKVLAF
RDITPQGPVH ILLIPKVRDG LTGLSKAEER HIDILGRLLY TAKLVAKQEG LAEGFRIVIN
DGPQGCQSVY HIHVHLIGGR QMNWPPG
