GATA_SORBI
ID GATA_SORBI Reviewed; 541 AA.
AC C5Y8Z8;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A, chloroplastic/mitochondrial {ECO:0000255|HAMAP-Rule:MF_03150};
DE Short=Glu-AdT subunit A {ECO:0000255|HAMAP-Rule:MF_03150};
DE EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_03150};
GN Name=GATA {ECO:0000255|HAMAP-Rule:MF_03150}; OrderedLocusNames=Sb06g030390;
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623;
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman M.,
RA Ware D., Westhoff P., Mayer K.F.X., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
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_03150}.
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; EC=6.3.5.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03150};
CC -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC complex, composed of A, B and C subunits. {ECO:0000255|HAMAP-
CC Rule:MF_03150}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03150}.
CC Plastid, chloroplast stroma {ECO:0000255|HAMAP-Rule:MF_03150}.
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_03150}.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03150}.
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DR EMBL; CM000765; EES11532.1; -; Genomic_DNA.
DR RefSeq; XP_002447204.1; XM_002447159.1.
DR AlphaFoldDB; C5Y8Z8; -.
DR SMR; C5Y8Z8; -.
DR STRING; 4558.Sb06g030390.1; -.
DR EnsemblPlants; EES11532; EES11532; SORBI_3006G237100.
DR GeneID; 8079563; -.
DR Gramene; EES11532; EES11532; SORBI_3006G237100.
DR KEGG; sbi:8079563; -.
DR eggNOG; KOG1211; Eukaryota.
DR HOGENOM; CLU_009600_0_3_1; -.
DR InParanoid; C5Y8Z8; -.
DR OMA; EVSCPHF; -.
DR OrthoDB; 1195292at2759; -.
DR Proteomes; UP000000768; Chromosome 6.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProt.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IEA:UniProtKB-UniRule.
DR GO; GO:0032543; P:mitochondrial translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.1300.10; -; 1.
DR HAMAP; MF_00120; GatA; 1.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR004412; GatA.
DR PANTHER; PTHR11895; PTHR11895; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR TIGRFAMs; TIGR00132; gatA; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chloroplast; Ligase; Mitochondrion; Nucleotide-binding;
KW Plastid; Protein biosynthesis; Reference proteome.
FT CHAIN 1..541
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000413343"
FT ACT_SITE 121
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 196
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 220
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
SQ SEQUENCE 541 AA; 56973 MW; 3FA7F172C9D75897 CRC64;
MPPPLQAHRL LISHRRLPSP ARRRFTAASS LQSAPATTLA PGPATSSILS IRESLLSGER
TAADITSEYL SRLRRTEPSL RSFIHVADAA AEREAEELDR RIASGEKDAV GPLAGVLVGV
KDNLCTANMP STGGSRILDG YRPAYDATAV RRLQEAGAIV VGKTNLDEFG MGSTTEGSAF
QVTTNPWDDS RVPGGSSGGS ASAVSARQCV VSLGSDTGGS VRQPASFCGV VGLKPTYGRV
SRFGLMAYAS SLDVVGCFGS SVFDTATILS VVAGHDKMDS TSSSQVVPDY ASELVSLDLL
ESKPLAGLRI GIIQETLGEG VANGVISSIK GAASHLEQLG SVVEEVSLPS FSLGLPAYYI
LASSEASSNL SRYDGIRYGR QFSADDLNEL YGESRANGLG HEVKMRILMG TYALSAGYYD
AYYKRAQQVR TLVKESFKDA LERYDILISP AAPSAAYKIG EKINDPLAMY AGDILTVNVN
LAGLPALVVP CGFVEGGPAG LPVGLQLIGS PFCEGNLLRV GHIFEQTLQN LSFVPPLLAE
S
