ID U5D321_AMBTC Unreviewed; 548 AA.
AC U5D321;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B, chloroplastic/mitochondrial {ECO:0000256|HAMAP-Rule:MF_03147};
DE Short=Glu-AdT subunit B {ECO:0000256|HAMAP-Rule:MF_03147};
DE EC=6.3.5.- {ECO:0000256|HAMAP-Rule:MF_03147};
GN Name=GATB {ECO:0000256|HAMAP-Rule:MF_03147};
GN ORFNames=AMTR_s00039p00150510 {ECO:0000313|EMBL:ERN15817.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN15817.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
CC -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or
CC Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn)
CC or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-
CC tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the
CC presence of glutamine and ATP through an activated phospho-Asp-
CC tRNA(Asn) or phospho-Glu-tRNA(Gln). {ECO:0000256|ARBA:ARBA00024799}.
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:0000256|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:0000256|ARBA:ARBA00000924, ECO:0000256|HAMAP-
CC Rule:MF_03147};
CC -!- SUBUNIT: Heterotrimer of A, B and C subunits.
CC {ECO:0000256|ARBA:ARBA00011123}.
CC -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC complex, composed of A, B and C subunits. {ECO:0000256|HAMAP-
CC Rule:MF_03147}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03147}.
CC Plastid, chloroplast {ECO:0000256|HAMAP-Rule:MF_03147}.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC {ECO:0000256|ARBA:ARBA00005306, ECO:0000256|HAMAP-Rule:MF_03147}.
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DR EMBL; KI392495; ERN15817.1; -; Genomic_DNA.
DR RefSeq; XP_006854350.1; XM_006854288.2.
DR AlphaFoldDB; U5D321; -.
DR STRING; 13333.U5D321; -.
DR EnsemblPlants; ERN15817; ERN15817; AMTR_s00039p00150510.
DR GeneID; 18444110; -.
DR Gramene; ERN15817; ERN15817; AMTR_s00039p00150510.
DR KEGG; atr:18444110; -.
DR eggNOG; KOG2438; Eukaryota.
DR HOGENOM; CLU_019240_0_0_1; -.
DR OMA; ARKWWMG; -.
DR OrthoDB; 5474932at2759; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; 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; 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; GatB domain, N-terminal subdomain; 1.
DR HAMAP; MF_00121; GatB; 1.
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; IPR004413; GatB.
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 NCBIfam; TIGR00133; gatB; 1.
DR PANTHER; PTHR11659; GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED; 1.
DR PANTHER; PTHR11659:SF0; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT B, MITOCHONDRIAL; 1.
DR Pfam; PF02934; GatB_N; 1.
DR Pfam; PF02637; GatB_Yqey; 1.
DR SMART; SM00845; GatB_Yqey; 1.
DR SUPFAM; SSF89095; GatB/YqeY motif; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS01234; GATB; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03147}; Chloroplast {ECO:0000256|HAMAP-Rule:MF_03147};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03147};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03147};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03147}; Plastid {ECO:0000256|HAMAP-Rule:MF_03147};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03147}; Reference proteome {ECO:0000313|Proteomes:UP000017836}.
FT DOMAIN 397..544
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
FT REGION 38..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 60582 MW; C4A942D08F16279C CRC64;
MASSSLFLRL PKSTLLFLSP LPLSTKHITS FCTKPKTQTL SSLSTNPSSP LRTKTQSHAP
LENPTLDYEP VIGIETHVQL STKTKAFCGC PSSYGSQPNT SICPICMGLP GSLPVLNSKV
IEFAVKLGLA LNCEISLRSK FDRKQYFYPD LPKGYQISQF DVPIARNGFT DLDLPCEFGG
GHRRFGITRV HMEEDAGKLI HSSNGDFSQV DLNRAGVPLL EIVSEPDMRS GIEAAEYAAE
IQRVVRYLGV SNGNMQEGSL RCDVNVSVRR KGQSVFGTKV EIKNMNSFSA MHRAIDFEIS
RQVSLLKEGK SDEVIQETRL WEEGAQRTVT MRKKEGLADY RYFPEPDLPE VILTEEYVNS
LGSGLPELPE MKRRRYEKMG LSMQDVLFLA DDFNVADFFD AAVGHGADVK LAANWVMSDI
AAYLKNEKLS ITEIKLTPME LAELIASIKN GTINGKIGKE ILFELIANGG TVGAMIEEKD
LVQIMDPNVI EAMIDKALAE NPKQLEQYRG GKTKLQGFFA GQVMKVSKGK ANPVLLNKLL
LEKLNAKS
//
