GATB_YEAST
ID GATB_YEAST Reviewed; 541 AA.
AC P33893; D6VPS3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 170.
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 AltName: Full=Cytochrome c oxidase assembly factor PET112;
GN Name=PET112 {ECO:0000255|HAMAP-Rule:MF_03147}; OrderedLocusNames=YBL080C;
GN ORFNames=YBL0724;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8082172; DOI=10.1007/bf00351481;
RA Mulero J.J., Rosenthal J.K., Fox T.D.;
RT "PET112, a Saccharomyces cerevisiae nuclear gene required to maintain rho+
RT mitochondrial DNA.";
RL Curr. Genet. 25:299-304(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7502586; DOI=10.1002/yea.320111112;
RA Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT cerevisiae chromosome II.";
RL Yeast 11:1103-1112(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 415.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [7]
RP FUNCTION, INTERACTION WITH HER2 AND YGR102C, AND SUBCELLULAR LOCATION.
RX PubMed=19417106; DOI=10.1101/gad.518109;
RA Frechin M., Senger B., Braye M., Kern D., Martin R.P., Becker H.D.;
RT "Yeast mitochondrial Gln-tRNA(Gln) is generated by a GatFAB-mediated
RT transamidation pathway involving Arc1p-controlled subcellular sorting of
RT cytosolic GluRS.";
RL Genes Dev. 23:1119-1130(2009).
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, ECO:0000269|PubMed:19417106}.
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 (HER2), B (PET112) and F (YGR102C) subunits.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03147,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:19417106}.
CC -!- MISCELLANEOUS: Present with 1390 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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}.
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DR EMBL; L22072; AAC37508.1; -; Genomic_DNA.
DR EMBL; X79489; CAA56028.1; -; Genomic_DNA.
DR EMBL; Z35841; CAA84901.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07043.2; -; Genomic_DNA.
DR PIR; S45428; S45428.
DR RefSeq; NP_009473.2; NM_001178320.2.
DR PDB; 4N0H; X-ray; 1.95 A; B=16-329.
DR PDB; 4N0I; X-ray; 2.00 A; B=16-329.
DR PDBsum; 4N0H; -.
DR PDBsum; 4N0I; -.
DR AlphaFoldDB; P33893; -.
DR SMR; P33893; -.
DR BioGRID; 32623; 64.
DR ComplexPortal; CPX-416; Glutamyl-tRNA(Gln) amidotransferase complex.
DR DIP; DIP-5011N; -.
DR IntAct; P33893; 4.
DR STRING; 4932.YBL080C; -.
DR MaxQB; P33893; -.
DR PaxDb; P33893; -.
DR PRIDE; P33893; -.
DR EnsemblFungi; YBL080C_mRNA; YBL080C; YBL080C.
DR GeneID; 852198; -.
DR KEGG; sce:YBL080C; -.
DR SGD; S000000176; PET112.
DR VEuPathDB; FungiDB:YBL080C; -.
DR eggNOG; KOG2438; Eukaryota.
DR GeneTree; ENSGT00390000016644; -.
DR HOGENOM; CLU_019240_4_0_1; -.
DR InParanoid; P33893; -.
DR OMA; ARKWWMG; -.
DR BioCyc; YEAST:G3O-28971-MON; -.
DR PRO; PR:P33893; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P33893; protein.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IDA:SGD.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT CHAIN 1..541
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit B,
FT mitochondrial"
FT /id="PRO_0000010712"
FT CONFLICT 415
FT /note="P -> A (in Ref. 2; CAA56028 and 3; CAA84901)"
FT /evidence="ECO:0000305"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:4N0H"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:4N0H"
FT TURN 66..70
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 80..93
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 142..157
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 196..212
FT /evidence="ECO:0007829|PDB:4N0H"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 224..233
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 247..263
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:4N0I"
FT HELIX 313..321
FT /evidence="ECO:0007829|PDB:4N0H"
SQ SEQUENCE 541 AA; 61869 MW; F426E82F1532B07D CRC64;
MLRLARFYSL ARTKAIHSHG APFRPEYALK CGLEIHTQLN TKNKLFSQST NSATSLVDAP
NHHTSYYDIA LPGTQPVLNL EAILFAMKLS LALGSQVNSI SQFDRKHYFY GDQPQGYQLT
QHYRPFARGG KINLSKELDD IDESAKEIGI LQLQIEQDTG KSHYTETDKD VITLVDLNRS
NVPLIELVTK PDFSDIKQVR AFIKKYQNLV RHLHISSGDL ETGAMRVDVN LSINEYARVE
LKNLPNTSSI INAIKYEYQR QVELISVGDT SSLMEPETRG WTGSSTVKLR SKETTIDYRY
MPDPELPYIN LAPDVISGVR GLMPQLPDDI MRILMKKPYQ LSLKDAKILT YNSNQNDMYN
HEALRSYYLD TFREFSKLAG ERSNAKLPTN WIIHEFLGDL NKLQIPLAKA KEILPPPVFA
QFLKLLHEEV ISATSGKMLL FHILENFEQS NCQDLSIPDF SKLIEKFELH AINQVDPQEL
MDLCNDVIAQ HTDDTFIRNL VTGKKKSSLK FLIGQGMRRS QGRIKANEFE KKFKEILNIQ
W
