ID A0A371FA96_MUCPR Unreviewed; 535 AA.
AC A0A371FA96;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B, chloroplastic/mitochondrial {ECO:0000313|EMBL:RDX75224.1};
DE Flags: Fragment;
GN Name=GATB {ECO:0000313|EMBL:RDX75224.1};
GN ORFNames=CR513_44919 {ECO:0000313|EMBL:RDX75224.1};
OS Mucuna pruriens (Velvet bean) (Dolichos pruriens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Mucuna.
OX NCBI_TaxID=157652 {ECO:0000313|EMBL:RDX75224.1, ECO:0000313|Proteomes:UP000257109};
RN [1] {ECO:0000313|EMBL:RDX75224.1, ECO:0000313|Proteomes:UP000257109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jos {ECO:0000313|Proteomes:UP000257109};
RC TISSUE=Seed {ECO:0000313|EMBL:RDX75224.1};
RA Nnadi N.E., Vos R., Hasami M.H., Devisetty U.K., Aguiy J.C.;
RT "Draft genome of Mucuna pruriens seed.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- 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};
CC -!- SUBUNIT: Heterotrimer of A, B and C subunits.
CC {ECO:0000256|ARBA:ARBA00011123}.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC {ECO:0000256|ARBA:ARBA00005306}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDX75224.1}.
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DR EMBL; QJKJ01009892; RDX75224.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371FA96; -.
DR STRING; 157652.A0A371FA96; -.
DR Proteomes; UP000257109; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Transferase {ECO:0000313|EMBL:RDX75224.1}.
FT DOMAIN 384..531
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
FT REGION 34..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RDX75224.1"
SQ SEQUENCE 535 AA; 59657 MW; F45E803E6EED2A17 CRC64;
MASTIFRSLQ VQPFLLYPTT LLRRRNGVFH LTTKATQSQT ETQQRQPQSK VSTSTQSKKL
DRIPKDYEAI IGIETHVQLS TLTKAFCGCP YNYGSPPNSS ICPICMGLPG ALPVLNSKVI
EFAVKLGLAL NCNLAFNSKF DRKQYFYPDL PKGYQISQFD VPIAAAGFLD VDIPVEFGGG
HKRFGITRVH MEEDAGKLLH AENGNYSQVD LNRAGVPLLE IVSEPDMRNG IEAAEYAAEI
QRLVRYLGVS NGNMQEGSLR CDVNVSIRPI GQSKFGTKVE IKNLNSFSSM NRAIDFEISR
QVQLHSQGQE DQIRTITMRK KEGLADYRYF PEPDLPAVIL SQEYVDGLKD SLPELPEIKR
RRYEQMGLSM QDVLFLANDK NIAEFFDATL VKGADPKLVA NWIMSDIAAY MKNEKLTINE
IKLTPEELSE LIASIKGGTI SGKIGKEILF ELLAKGGSVK ELIEKKDLVQ IVDPVEIEKM
VDKVIAENPK QLEQYRGGKT KLQGFFAGQV MKLSKGKANP GLLNKILLEK LNSKS
//
