GATB_ARATH
ID GATB_ARATH Reviewed; 550 AA.
AC Q9FV81; F4HYH2; Q9LP72;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B, chloroplastic/mitochondrial {ECO:0000255|HAMAP-Rule:MF_03147};
DE Short=Glu-AdT subunit B {ECO:0000255|HAMAP-Rule:MF_03147};
DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_03147};
GN Name=GATB {ECO:0000255|HAMAP-Rule:MF_03147}; OrderedLocusNames=At1g48520;
GN ORFNames=T1N15.14;
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 [MRNA] (ISOFORM 1).
RA Chang W., Soll D.;
RT "Arabidopsis thaliana Glu-tRNA(Gln) amidotransferase B subunit (gat B).";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18441100; DOI=10.1073/pnas.0712299105;
RA Pujol C., Bailly M., Kern D., Marechal-Drouard L., Becker H.,
RA Duchene A.-M.;
RT "Dual-targeted tRNA-dependent amidotransferase ensures both mitochondrial
RT and chloroplastic Gln-tRNAGln synthesis in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6481-6485(2008).
CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC through the transamidation of misacylated Glu-tRNA(Gln) in chloroplasts
CC and mitochondria. The reaction takes place in the presence of glutamine
CC and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
CC {ECO:0000255|HAMAP-Rule:MF_03147, ECO:0000269|PubMed:18441100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03147};
CC -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC complex, composed of A, B and C subunits. {ECO:0000255|HAMAP-
CC Rule:MF_03147}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03147,
CC ECO:0000269|PubMed:18441100}. Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_03147, ECO:0000269|PubMed:18441100}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FV81-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FV81-2; Sequence=VSP_041875, VSP_041876;
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_03147}.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03147}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79700.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BX815942; Type=Miscellaneous discrepancy; Note=Sequencing errors.; 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; AF239836; AAG29096.1; -; mRNA.
DR EMBL; AC020889; AAF79700.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32307.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32309.1; -; Genomic_DNA.
DR EMBL; AY054223; AAL06883.1; -; mRNA.
DR EMBL; AY074557; AAL67097.1; -; mRNA.
DR EMBL; BX815942; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK227161; BAE99203.1; -; mRNA.
DR RefSeq; NP_564530.1; NM_103748.3. [Q9FV81-1]
DR RefSeq; NP_973990.1; NM_202261.2. [Q9FV81-2]
DR AlphaFoldDB; Q9FV81; -.
DR SMR; Q9FV81; -.
DR BioGRID; 26498; 2.
DR IntAct; Q9FV81; 1.
DR STRING; 3702.AT1G48520.1; -.
DR PaxDb; Q9FV81; -.
DR PRIDE; Q9FV81; -.
DR ProteomicsDB; 222158; -. [Q9FV81-1]
DR EnsemblPlants; AT1G48520.1; AT1G48520.1; AT1G48520. [Q9FV81-1]
DR EnsemblPlants; AT1G48520.2; AT1G48520.2; AT1G48520. [Q9FV81-2]
DR GeneID; 841273; -.
DR Gramene; AT1G48520.1; AT1G48520.1; AT1G48520. [Q9FV81-1]
DR Gramene; AT1G48520.2; AT1G48520.2; AT1G48520. [Q9FV81-2]
DR KEGG; ath:AT1G48520; -.
DR Araport; AT1G48520; -.
DR TAIR; locus:2198045; AT1G48520.
DR eggNOG; KOG2438; Eukaryota.
DR HOGENOM; CLU_019240_0_0_1; -.
DR InParanoid; Q9FV81; -.
DR OMA; ARKWWMG; -.
DR PhylomeDB; Q9FV81; -.
DR BioCyc; ARA:AT1G48520-MON; -.
DR PRO; PR:Q9FV81; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FV81; baseline and differential.
DR Genevisible; Q9FV81; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IBA:GO_Central.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR Gene3D; 1.10.10.410; -; 1.
DR HAMAP; MF_00121; GatB; 1.
DR InterPro; IPR004413; Apn/Gln-ADT_bsu.
DR InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E.
DR InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat.
DR InterPro; IPR018027; Asn/Gln_amidotransferase.
DR InterPro; IPR003789; Asn/Gln_tRNA_amidoTrase-B-like.
DR InterPro; IPR023168; GatB_Yqey_C_2.
DR InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11659; PTHR11659; 1.
DR Pfam; PF02934; GatB_N; 1.
DR Pfam; PF02637; GatB_Yqey; 1.
DR SMART; SM00845; GatB_Yqey; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR SUPFAM; SSF89095; SSF89095; 1.
DR TIGRFAMs; TIGR00133; gatB; 1.
DR PROSITE; PS01234; GATB; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Chloroplast; Ligase; Mitochondrion;
KW Nucleotide-binding; Plastid; Protein biosynthesis; Reference proteome.
FT CHAIN 1..550
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit B,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000413224"
FT REGION 32..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 463..475
FT /note="ILFELLAKGGTVK -> VGSIQSTNSSSFA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_041875"
FT VAR_SEQ 476..550
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_041876"
SQ SEQUENCE 550 AA; 60941 MW; 1648674FCBE68087 CRC64;
MSTTLLRTIQ LNQFSLLGTS LLRRRRSNNF SVRSCGSQTT TTHEAKQSSP TRVAPKNHKS
NQLDEILRDY EAVIGIETHV QLSTLTKAFC SCSNNYGSYP NTSICPVCMG LPGALPVLNS
KVVEFGVRLG LALNCDLSLK SKFDRKQYFY PDLPKGYQIS QFDIPIASGG YVDVDIPLEF
GGGHRRFGIT RVHMEEDAGK LLHSDTGDYS QVDLNRAGVP LLEIVSEPDM RSGIEAAEYA
CEMQRIARYL GVSNGNMQEG SLRCDVNISI RPIGQAEFGT KVEIKNLNAF SAISRAIDFE
ISRQALLYNQ GKADQIVTET RLWEEGAQKT VTMRKKEGLA DYRYFPEPDL PEVILTQEYV
DSIRASLPEL PEAKRRRYEA MGLGMQDVLF LANDVSVAEY FDAVIGKGAE VKLAANWIMS
DIAAYLKNEK LSINDIKLTP QELAELIAAI KDGTISGKIG KEILFELLAK GGTVKGMIKA
KDLVQITDPA EIEKMVIQVV SENPKQLEQY RSGKTKLQGY FAGQVMKMSK GKANPGLLNK
ILLEKLNAKD
