ID   A0A099Z513_TINGU        Unreviewed;       493 AA.
AC   A0A099Z513;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   13-SEP-2023, entry version 25.
DE   RecName: Full=Asn/Gln amidotransferase domain-containing protein {ECO:0000259|SMART:SM00845};
DE   Flags: Fragment;
GN   ORFNames=N309_10448 {ECO:0000313|EMBL:KGL76188.1};
OS   Tinamus guttatus (White-throated tinamou).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX   NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL76188.1, ECO:0000313|Proteomes:UP000053641};
RN   [1] {ECO:0000313|EMBL:KGL76188.1, ECO:0000313|Proteomes:UP000053641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL76188.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC       {ECO:0000256|ARBA:ARBA00005306}.
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DR   EMBL; KL888753; KGL76188.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099Z513; -.
DR   STRING; 94827.A0A099Z513; -.
DR   Proteomes; UP000053641; Unassembled WGS sequence.
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:0006412; P:translation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.410; -; 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; IPR023168; GatB_Yqey_C_2.
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.
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   Reference proteome {ECO:0000313|Proteomes:UP000053641}.
FT   DOMAIN          344..493
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGL76188.1"
FT   NON_TER         493
FT                   /evidence="ECO:0000313|EMBL:KGL76188.1"
SQ   SEQUENCE   493 AA;  55357 MW;  5272269F27A9A084 CRC64;
     WLPVVGLEIH AQISSNSKLF SGSQVQFAAP PNSLVSFFDA SLPGTLPVLN RRCVEAAVMT
     GLALNCSINK KSLFDRKHYF YADLPAGYQI TQKRVPIAVN GSLSYSLCID NKMSRMVTKT
     VRIKQIQLEQ DSGKSLHDDT RSQTLVDLNR AGVGLMEVVM EPDMCCGEEA AAAVRELQLI
     LQTLGSSKAI MAEGQLRVDA NVSVHHPGEP YGVRTEVKNI NSVRFLAKAI DYEIQRQIEE
     LENGGTILNE TRAFDSKLGC TISMRDKEGK QDYRFMPEPN LPPLILYDAK SLPANRNHQQ
     VVNIDWIRER LPDLPSVKRA KLVELYGILP EHSFTLLNED GLAEYFENVI KHTQMKPKKV
     IGWVLKELLS YLKEHALAVK DSPVSSFLLA DLLNLLERKE ISSSAAKQVF EELWKGEGKT
     PLEIVKEKHL ELLRDQEELE QICQAVIDRQ EDEVMAIKAG NQKVLNKLIG LVQRATRGRS
     NPVLVKQILE KKL
//