(data stored in ACNUC7421 zone)

SWISSPROT: GATB_ASHGO

ID   GATB_ASHGO              Reviewed;         536 AA.
AC   Q751Q9;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 95.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B, 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};
DE   Flags: Precursor;
GN   Name=PET112 {ECO:0000255|HAMAP-Rule:MF_03147}; OrderedLocusNames=AGL303W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in the
CC       mitochondria. The reaction takes place in the presence of glutamine and
CC       ATP through an activated gamma-phospho-Glu-tRNA(Gln).
CC       {ECO:0000255|HAMAP-Rule:MF_03147}.
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 GatFAB amidotransferase (AdT)
CC       complex, composed of A, B and F subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_03147}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03147}.
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03147}.
DR   EMBL; AE016820; AAS54188.1; -; Genomic_DNA.
DR   RefSeq; NP_986364.1; NM_211426.1.
DR   SMR; Q751Q9; -.
DR   STRING; 33169.AAS54188; -.
DR   PRIDE; Q751Q9; -.
DR   EnsemblFungi; AAS54188; AAS54188; AGOS_AGL303W.
DR   GeneID; 4622657; -.
DR   KEGG; ago:AGOS_AGL303W; -.
DR   HOGENOM; HOG000223742; -.
DR   InParanoid; Q751Q9; -.
DR   KO; K02434; -.
DR   OMA; ARKWWMG; -.
DR   Proteomes; UP000000591; Chromosome VII.
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   Gene3D; 1.10.150.380; -; 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; IPR042114; GatB_C_1.
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   3: Inferred from homology;
DR   PRODOM; Q751Q9.
DR   SWISS-2DPAGE; Q751Q9.
KW   ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome; Transit peptide.
FT   TRANSIT         1..8
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03147"
FT   CHAIN           9..536
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit B,
FT                   mitochondrial"
FT                   /id="PRO_0000413242"
SQ   SEQUENCE   536 AA;  60820 MW;  34EDAF3EB02A126C CRC64;
     MLRVHRLYST RGAAEVLHAA PKYALRCGLE IHTQLNTRNK LFSLSTNDPF QAAATPNYHT
     SFFDISLPGT QPRLNYEAVL YAIKLSLALD CRVNLKSQFD RKHYFYGDQP LGYQITQHYN
     PIAKDGKLCL YGAYDNIPED EKTIGIIQLQ LEQDTGRSLY KDTDGMTLID LNRSNVPLVE
     MVTQPDFTDV KQVRAFVKKY QNLVRHLNIS TGDLETGAMR VDVNMSVNGH ARVELKNLPN
     TSSITNAIRY EYQRQVDIIR SGQADKMLKD VETRGWTGSA TIKLRSKEST IDYRYMPDPE
     IPVLLLEPEV VHRVATALPE LPDQTLRKLM AEPYNLSLKD AKILTTNSNS HGNFYTHHDL
     RNYFMKTFQL FTAKTGASNS KLPANWIIHE LLGIINKLEI PLPKILQLLP ASHFAEFLAL
     IHDNELSKSS AKLLLFHIIN DFKESHCSNL ALPDFRLLIE QYNLNPLNEV EEHALTELCQ
     YVLRELNDDA LVADLVSGKK KNALKFLLGK GMRLSQGKVD PALLEGAFKS VLGIKW
//

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