GATB_EMENI
ID GATB_EMENI Reviewed; 602 AA.
AC Q33446; C8VJ83; Q5B980;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 3.
DT 25-MAY-2022, entry version 115.
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 AltName: Full=Protein NEMPA;
DE Flags: Precursor;
GN Name=nempA; ORFNames=AN2900;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Swigut T.;
RT "Cloning and analysis of the yeast pet112 homolog from the Emericella
RT nidulans.";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(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 GatCAB amidotransferase (AdT)
CC complex, composed of A, B and C subunits. {ECO:0000255|HAMAP-
CC Rule:MF_03147}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03147}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB05037.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U62332; AAB05037.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AACD01000051; EAA63471.1; -; Genomic_DNA.
DR EMBL; BN001306; CBF83785.1; -; Genomic_DNA.
DR RefSeq; XP_660504.1; XM_655412.1.
DR AlphaFoldDB; Q33446; -.
DR SMR; Q33446; -.
DR STRING; 162425.CADANIAP00010189; -.
DR EnsemblFungi; CBF83785; CBF83785; ANIA_02900.
DR EnsemblFungi; EAA63471; EAA63471; AN2900.2.
DR GeneID; 2873984; -.
DR KEGG; ani:AN2900.2; -.
DR VEuPathDB; FungiDB:AN2900; -.
DR eggNOG; KOG2438; Eukaryota.
DR HOGENOM; CLU_019240_4_1_1; -.
DR InParanoid; Q33446; -.
DR OMA; ARKWWMG; -.
DR OrthoDB; 898782at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IBA:GO_Central.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
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; Transit peptide.
FT TRANSIT 1..56
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03147"
FT CHAIN 57..602
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit B,
FT mitochondrial"
FT /id="PRO_0000010713"
FT CONFLICT 291
FT /note="V -> L (in Ref. 1; AAB05037)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="E -> D (in Ref. 1; AAB05037)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="E -> Q (in Ref. 1; AAB05037)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="E -> D (in Ref. 1; AAB05037)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="R -> P (in Ref. 1; AAB05037)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="R -> S (in Ref. 1; AAB05037)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="Missing (in Ref. 1; AAB05037)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="A -> R (in Ref. 1; AAB05037)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 602 AA; 67207 MW; CF1867C8D02379DD CRC64;
MFRSCLRHCR RATVRSRTCP RCSHHEIPQL QVVQRQISLS SSFPHIRRLQ TSSTDTQERI
PIRKQLKQEA KAIKSRKRER REQEEASRHK WELTVGVEIH AQLNTETKLF SRAPTSPSEL
PNTNVALFDL AFPGSQPEFQ VATLLPALRA AIALNCDIQP VSRFDRKHYF YQDQPSGYQI
TQYYEPFARN GYLDLFRHDG IAPEDGDRVR IGIKQIQLEQ DTAKSQEYPP SMQLLDFNRV
SHPLIEIITM PEIHTPATAA AFVRKVQAIL QSCSAVTTGM EAGGLRADIN VSVRLRGDGS
GTHQYSGIGG LGQRTEIKNL SSFKAVEDAI IAEKNRQIAV LESGGVVEGE TRGWTIGSTE
TRKLRGKEGE VDYRYMPDPD IPPLLIGKDI ISALSNTLPA GPDALIDMLV GQYGLAIEDA
KPLVELEDGA RLEYYQDVVD ILRNLQQDLD SKTQAGLGRV AGNWVLHELG GLLSKAGLAW
DAERVTAESL AALIDQLQRK RITGATAKKV LAMLFDGDRR PVAQLLEEEN LILRPLSREE
YIALASAAIE LNPQMVEQIR SKNQLGKLGW FVGQMMRMGE KGRVEAQKAD AILRELILGL
SQ
