ID   GATB_KOMPG              Reviewed;         492 AA.
AC   C4R8P2;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 65.
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};
GN   Name=PET112 {ECO:0000255|HAMAP-Rule:MF_03147};
GN   OrderedLocusNames=PAS_chr4_0705;
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864;
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
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 GatFAB amidotransferase (AdT)
CC       complex, composed of A, B and F subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_03147}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03147}.
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC       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; FN392322; CAY71967.1; -; Genomic_DNA.
DR   RefSeq; XP_002494146.1; XM_002494101.1.
DR   AlphaFoldDB; C4R8P2; -.
DR   SMR; C4R8P2; -.
DR   STRING; 644223.C4R8P2; -.
DR   PRIDE; C4R8P2; -.
DR   EnsemblFungi; CAY71967; CAY71967; PAS_chr4_0705.
DR   GeneID; 8200601; -.
DR   KEGG; ppa:PAS_chr4_0705; -.
DR   eggNOG; KOG2438; Eukaryota.
DR   HOGENOM; CLU_019240_4_0_1; -.
DR   InParanoid; C4R8P2; -.
DR   OMA; ARKWWMG; -.
DR   Proteomes; UP000000314; Chromosome 4.
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; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
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.
DR   PROSITE; PS01234; GATB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..492
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit B,
FT                   mitochondrial"
FT                   /id="PRO_0000413272"
SQ   SEQUENCE   492 AA;  56042 MW;  190D1A60379F1E6C CRC64;
     MLRKLVCGLE IHTQLKTGQK LFSLSSTEAS KPNTNISFFD IGLPGSQPTL NQACLLTALK
     ACVSLNSNIN SVSTFDRKHY FYPDQPNGYQ ITQYYRPISS GGFLKLSKRF DEIDEDEKLV
     RIHHIQIEQD TGKSLYKDLS DKSLVDYNRS NMPLIEVVTE PDLNSVKQVK AFLRKYLQLM
     KTMDVSTGQL EAGAMRVDVN VSVDDGERVE IKNMTSTSAI VNAIRYEFKR QTKSIDKGNP
     IKTKETRGWD GNKTFRLRDK ESSVDYRYMP DPELPPVVLD VNDIVTRIKK MTITTPEEQL
     AQLMSPPYNI KLRDARILLN DRNLLGYYYA LFSRTSAKNI PSKYPINWCC HEFLGYLAKN
     NIDFSEDLFP VHQLADLIDC IFREQVTNNN AKILFEHLLA NPAENEGPII DLITKYELGE
     VDVTNDSELL AQVDSIIDDV LDTYPAIVKE LQEGNKPGSI NYLLGQCMRT SAGRIKSKVF
     ESRLKEKIHI IK