ID   A0A087R9S9_APTFO        Unreviewed;       495 AA.
AC   A0A087R9S9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   13-SEP-2023, entry version 20.
DE   RecName: Full=Asn/Gln amidotransferase domain-containing protein {ECO:0000259|SMART:SM00845};
DE   Flags: Fragment;
GN   ORFNames=AS27_12820 {ECO:0000313|EMBL:KFM10233.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM10233.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM10233.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM10233.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-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; KL226231; KFM10233.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087R9S9; -.
DR   STRING; 9233.A0A087R9S9; -.
DR   Proteomes; UP000053286; 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:UP000053286}.
FT   DOMAIN          344..493
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFM10233.1"
FT   NON_TER         495
FT                   /evidence="ECO:0000313|EMBL:KFM10233.1"
SQ   SEQUENCE   495 AA;  55379 MW;  F9447D147BA20991 CRC64;
     WVPVVGLEIH AQISSNSKLF SGSQVQFAAA PNSLVSFFDA SLPGTLPVLN RRCVEAAVMT
     GLALNCSINK RSLFDRKHYF YADLPAGYQI TQQRVPIAVN GSLSYSICID NKMSQMVTKT
     VRIKQIQLEQ DSGKSLHDDT RNQTLVDLNR AGVGLMEVVM EPDMCCGEEA AAAVRELQLI
     LQTLGSSQAV MAEGQLRVDA NISVHHPGEH YGVRTEVKNI NSLRFLAKAV DYEIQRQIEE
     LENGGTILNE TRAFDSKLGC TVPMRDKEGK QDYRFMPEPN LPPLILYDAK SLPANMNHQQ
     VVNVDWIHER LPDLPSVKRA KLVERYGILP EHGFTLLNED GLTEFFENVV KQTQMKPKKV
     IGWILNDLLS YLKQHSLTVK ESPVSSFLLA DLLNLLEKKE ISSTAAKQVL AELWKGEGKT
     PFEIVKEKKL ELIQDQKELE QICQAVIDGQ ENEVMAIKAG NQKVLNKLIG LVQRETQGRS
     NPALVKQLLE KKLSE
//