GSDA_ARATH
ID GSDA_ARATH Reviewed; 185 AA.
AC Q94BU8;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Guanosine deaminase {ECO:0000303|PubMed:24130159};
DE EC=3.5.4.15 {ECO:0000269|PubMed:24130159};
DE AltName: Full=tRNA-specific adenosine deaminase TAD4 {ECO:0000303|PubMed:25315605};
DE Short=AtTAD4 {ECO:0000303|PubMed:25315605};
GN Name=GSDA {ECO:0000303|PubMed:24130159};
GN Synonyms=TAD4 {ECO:0000303|PubMed:25315605};
GN OrderedLocusNames=At5g28050 {ECO:0000312|Araport:AT5G28050};
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=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;
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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24130159; DOI=10.1105/tpc.113.117184;
RA Dahncke K., Witte C.P.;
RT "Plant purine nucleoside catabolism employs a guanosine deaminase required
RT for the generation of xanthosine in Arabidopsis.";
RL Plant Cell 25:4101-4109(2013).
RN [5]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25315605; DOI=10.1104/pp.114.250498;
RA Zhou W., Karcher D., Bock R.;
RT "Identification of enzymes for adenosine-to-inosine editing and discovery
RT of cytidine-to-uridine editing in nucleus-encoded transfer RNAs of
RT Arabidopsis.";
RL Plant Physiol. 166:1985-1997(2014).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of guanosine, producing
CC xanthosine and ammonia. Deaminates exclusively guanosine and 2'-
CC deoxyguanosine but no other aminated purines, pyrimidines, or pterines.
CC Deamination of guanosine by GSDA is the only source of xanthosine
CC production in Arabidopsis. {ECO:0000269|PubMed:24130159}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine + H(+) + H2O = NH4(+) + xanthosine;
CC Xref=Rhea:RHEA:12861, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16750, ChEBI:CHEBI:18107, ChEBI:CHEBI:28938; EC=3.5.4.15;
CC Evidence={ECO:0000269|PubMed:24130159};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24130159,
CC ECO:0000269|PubMed:25315605}. Nucleus {ECO:0000269|PubMed:25315605}.
CC Note=Localizes predominantly to the nucleus.
CC {ECO:0000269|PubMed:25315605}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers and siliques.
CC {ECO:0000269|PubMed:24130159}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotyper under normal growth
CC conditions. {ECO:0000269|PubMed:25315605}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; AC007627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93768.1; -; Genomic_DNA.
DR EMBL; AY039873; AAK63977.1; -; mRNA.
DR EMBL; AY133663; AAM91493.1; -; mRNA.
DR RefSeq; NP_198157.1; NM_122688.4.
DR PDB; 7DBF; X-ray; 1.90 A; A/D=29-185.
DR PDB; 7DC9; X-ray; 1.70 A; A/D=29-185.
DR PDB; 7DCA; X-ray; 2.10 A; A/D=29-185.
DR PDB; 7DCB; X-ray; 2.00 A; A/D=29-185.
DR PDB; 7DCW; X-ray; 2.30 A; A/D=29-185.
DR PDB; 7DGC; X-ray; 2.10 A; A/D=29-185.
DR PDB; 7DH1; X-ray; 1.85 A; A/D=29-185.
DR PDB; 7DLC; X-ray; 2.45 A; A/D=29-185.
DR PDB; 7DM5; X-ray; 2.20 A; A/D=29-185.
DR PDB; 7DM6; X-ray; 2.05 A; A/D=29-185.
DR PDB; 7DOW; X-ray; 2.00 A; A/D=29-185.
DR PDB; 7DOX; X-ray; 1.90 A; A/D=29-185.
DR PDB; 7DOY; X-ray; 2.17 A; A/D=29-185.
DR PDB; 7DPK; X-ray; 2.15 A; A/D=29-185.
DR PDB; 7DQN; X-ray; 2.60 A; A/D=29-185.
DR PDBsum; 7DBF; -.
DR PDBsum; 7DC9; -.
DR PDBsum; 7DCA; -.
DR PDBsum; 7DCB; -.
DR PDBsum; 7DCW; -.
DR PDBsum; 7DGC; -.
DR PDBsum; 7DH1; -.
DR PDBsum; 7DLC; -.
DR PDBsum; 7DM5; -.
DR PDBsum; 7DM6; -.
DR PDBsum; 7DOW; -.
DR PDBsum; 7DOX; -.
DR PDBsum; 7DOY; -.
DR PDBsum; 7DPK; -.
DR PDBsum; 7DQN; -.
DR AlphaFoldDB; Q94BU8; -.
DR SMR; Q94BU8; -.
DR IntAct; Q94BU8; 1.
DR STRING; 3702.AT5G28050.2; -.
DR PRIDE; Q94BU8; -.
DR ProteomicsDB; 247222; -.
DR EnsemblPlants; AT5G28050.1; AT5G28050.1; AT5G28050.
DR GeneID; 832875; -.
DR Gramene; AT5G28050.1; AT5G28050.1; AT5G28050.
DR KEGG; ath:AT5G28050; -.
DR Araport; AT5G28050; -.
DR HOGENOM; CLU_025810_5_2_1; -.
DR OMA; SNAPFEA; -.
DR PhylomeDB; Q94BU8; -.
DR BRENDA; 3.5.4.15; 399.
DR PRO; PR:Q94BU8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94BU8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0047974; F:guanosine deaminase activity; IDA:UniProtKB.
DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006152; P:purine nucleoside catabolic process; IDA:UniProtKB.
DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IEA:InterPro.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR028883; tRNA_aden_deaminase.
DR Pfam; PF14437; MafB19-deam; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Metal-binding; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..185
FT /note="Guanosine deaminase"
FT /id="PRO_0000443861"
FT DOMAIN 28..142
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 82
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT HELIX 30..47
FT /evidence="ECO:0007829|PDB:7DC9"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:7DC9"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:7DC9"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:7DC9"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:7DC9"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:7DC9"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:7DC9"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:7DC9"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:7DC9"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:7DC9"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:7DC9"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:7DC9"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:7DCB"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:7DC9"
FT HELIX 165..177
FT /evidence="ECO:0007829|PDB:7DC9"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:7DC9"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:7DBF"
SQ SEQUENCE 185 AA; 20002 MW; 415F99A5B20371D9 CRC64;
MEEAKVEAKD GTISVASAFS GHQQAVHDSD HKFLTQAVEE AYKGVDCGDG GPFGAVIVHN
NEVVASCHNM VLKYTDPTAH AEVTAIREAC KKLNKIELSE CEIYASCEPC PMCFGAIHLS
RLKRLVYGAK AEAAIAIGFD DFIADALRGT GVYQKSSLEI KKADGNGAAI AEQVFQNTKE
KFRLY
