ID A0A164VV73_9AGAM Unreviewed; 515 AA.
AC A0A164VV73;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03150};
DE Short=Glu-AdT subunit A {ECO:0000256|HAMAP-Rule:MF_03150};
DE EC=6.3.5.7 {ECO:0000256|HAMAP-Rule:MF_03150};
GN ORFNames=SISNIDRAFT_549058 {ECO:0000313|EMBL:KZS94499.1};
OS Sistotremastrum niveocremeum HHB9708.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314777 {ECO:0000313|EMBL:KZS94499.1, ECO:0000313|Proteomes:UP000076722};
RN [1] {ECO:0000313|EMBL:KZS94499.1, ECO:0000313|Proteomes:UP000076722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB9708 {ECO:0000313|EMBL:KZS94499.1,
RC ECO:0000313|Proteomes:UP000076722};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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:0000256|HAMAP-Rule:MF_03150}.
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; EC=6.3.5.7;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03150};
CC -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC complex, composed of A, B and C subunits. {ECO:0000256|HAMAP-
CC Rule:MF_03150}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03150}.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03150}.
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DR EMBL; KV419404; KZS94499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164VV73; -.
DR STRING; 1314777.A0A164VV73; -.
DR OrthoDB; 4001253at2759; -.
DR Proteomes; UP000076722; 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; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR HAMAP; MF_00120; GatA; 1.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR004412; GatA.
DR PANTHER; PTHR11895:SF7; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03150};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03150};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03150};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03150};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03150}; Reference proteome {ECO:0000313|Proteomes:UP000076722}.
FT DOMAIN 56..499
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 59
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
FT ACT_SITE 136
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
FT ACT_SITE 160
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
SQ SEQUENCE 515 AA; 55679 MW; 3E35ED495630B009 CRC64;
MRSLLRENVR LLEKAKTARF FGTLTSSRHG SVNNSEINAF VSVNDNLANS ARGRRVAIKD
NICTKDFLTT CSSSILRTFD PGYDATLASL LKSRGWNIIG KTNCDEFGMG SLNVYSSHGP
VINPWNPSER RSAGGSSGGS AAAVAAGLCE AAIGTDTGGS TRLPAAYCGI IGFKPSHGLI
SRWGVVSYAD SLDCVGIFGK DAEIVSEVFE VLNVHDPQDP TSANSQVRER MQSQFVASKV
SNMSEKSFWS TVRVGIPLEY FPHELDPSLL KSYKNVLRLL LQRGAQLVPI SLPNTKYALS
AYYALSSAEA SSNMARYNGK LHGKLYPLLR YQIRILRVAV GEPASESSTR HRTPIDQYAA
NRTAGFGPEV QRRVLLGTYT LTADAFDNYF LQAMRVRSLV QQDFSSVFKM ADLRESSEDN
IGDSGVDFIL HLSAIRSAPQ LSETGQPGSE IDSYVQDVMT VPASLAGLPA ASIPSGLADD
DWPVGVSIVG QWGSDHLLLK ACKELTALLS VASNK
//
