ID   GATB_AEDAE              Reviewed;         528 AA.
AC   Q16UG2;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03147};
DE            Short=Glu-AdT subunit B {ECO:0000255|HAMAP-Rule:MF_03147};
DE            EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_03147};
DE   Flags: Precursor;
GN   ORFNames=AAEL009908;
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVPib12;
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA   Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA   Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA   Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA   Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA   El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA   Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA   Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA   Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA   Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA   Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA   Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA   Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(2007).
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in the
CC       mitochondria. The reaction takes place in the presence of glutamine and
CC       ATP through an activated gamma-phospho-Glu-tRNA(Gln).
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_03147};
CC   -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC       complex, composed of A, B and C subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_03147}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03147}.
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03147}.
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DR   EMBL; CH477622; EAT38175.1; -; Genomic_DNA.
DR   RefSeq; XP_001654104.1; XM_001654054.1.
DR   AlphaFoldDB; Q16UG2; -.
DR   SMR; Q16UG2; -.
DR   STRING; 7159.AAEL009908-PA; -.
DR   GeneID; 5572590; -.
DR   KEGG; aag:5572590; -.
DR   VEuPathDB; VectorBase:AAEL009908; -.
DR   eggNOG; KOG2438; Eukaryota.
DR   HOGENOM; CLU_019240_1_1_1; -.
DR   InParanoid; Q16UG2; -.
DR   OMA; ARKWWMG; -.
DR   OrthoDB; 898782at2759; -.
DR   PhylomeDB; Q16UG2; -.
DR   Proteomes; UP000008820; Unassembled WGS sequence.
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:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IEA:UniProtKB-UniRule.
DR   GO; GO:0032543; P:mitochondrial translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.410; -; 1.
DR   HAMAP; MF_00121; GatB; 1.
DR   InterPro; IPR004413; Apn/Gln-ADT_bsu.
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; IPR023168; GatB_Yqey_C_2.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   PANTHER; PTHR11659; PTHR11659; 1.
DR   Pfam; PF02934; GatB_N; 1.
DR   Pfam; PF02637; GatB_Yqey; 1.
DR   SMART; SM00845; GatB_Yqey; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   SUPFAM; SSF89095; SSF89095; 1.
DR   TIGRFAMs; TIGR00133; gatB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome; Transit peptide.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03147"
FT   CHAIN           22..528
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit B,
FT                   mitochondrial"
FT                   /id="PRO_0000413221"
SQ   SEQUENCE   528 AA;  58900 MW;  8908A70C7A99BAFB CRC64;
     MSWRLSFRTN LLIYNVRRRN YATKAAGKPA TRPNRWKSVI GLEVHAQIQT NSKLFSGAEV
     AFSSPINSCV SLFDASIPGT LPVLNRKCVE LGVRTALALG CKVNSVSMFD RKHYFYADLP
     AGYQITQQRA PLARGGLLSF PVFVPGVSRK PYYKSARLHQ LQLEQDSGKS LHDPVERKSL
     VDLNRAGVPL MELVFEPDLE TGEEAAALVK ELILILTRLG SCSCRMEEGA LRVDANISVH
     KENTPLGTRT EVKNIGSVRA VAQAIEFEIE RQIGILDGGG KIFNETRAWD AAGRQTIAMR
     DKEVVQDYRF MPEPNLPPLH VNVDGECDAD VVVDAVHIGS SLPELPEETR RQIVEIHNLT
     PEMAIILVND ITLYNHFRTI LDEPGKARSP KAVANFLINE LLTILNKNKI DIEECRIPST
     HLAEVTDMLE GNIINAYLAR LIVQEALDGE GRESPALLAQ RNDWLMITDT ERIEAMCKDA
     IKNNPKVVEK YRKGKEKMLY ALAGEIAKVS EQKVDMAKSV DLLKNMLK