GATB2_MICCC
ID GATB2_MICCC Reviewed; 529 AA.
AC C1FJ20;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B-2, chloroplastic/mitochondrial;
DE Short=Glu-AdT subunit B-2 {ECO:0000255|HAMAP-Rule:MF_03147};
DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_03147};
GN Name=GATB-2 {ECO:0000255|HAMAP-Rule:MF_03147}; ORFNames=MICPUN_87214;
OS Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Mamiellaceae; Micromonas.
OX NCBI_TaxID=296587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC299 / NOUM17;
RX PubMed=19359590; DOI=10.1126/science.1167222;
RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA Grigoriev I.V.;
RT "Green evolution and dynamic adaptations revealed by genomes of the marine
RT picoeukaryotes Micromonas.";
RL Science 324:268-272(2009).
CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC through the transamidation of misacylated Glu-tRNA(Gln) in chloroplasts
CC and mitochondria. The reaction takes place in the presence of glutamine
CC and 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 Plastid, chloroplast {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; CP001577; ACO70513.1; -; Genomic_DNA.
DR RefSeq; XP_002509255.1; XM_002509209.1.
DR AlphaFoldDB; C1FJ20; -.
DR SMR; C1FJ20; -.
DR STRING; 296587.XP_002509255.1; -.
DR GeneID; 8248140; -.
DR KEGG; mis:MICPUN_87214; -.
DR eggNOG; KOG2438; Eukaryota.
DR InParanoid; C1FJ20; -.
DR OMA; QLEMDTG; -.
DR OrthoDB; 898782at2759; -.
DR Proteomes; UP000002009; Chromosome 12.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; 2.
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; Chloroplast; Ligase; Mitochondrion; Nucleotide-binding;
KW Plastid; Protein biosynthesis; Reference proteome.
FT CHAIN 1..529
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit B-2,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000413228"
FT REGION 17..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 529 AA; 56028 MW; 2446F57C3B6B98AB CRC64;
MLRRALASRS SEAAIISTRV SLPRGSIPPP PTSSSSSSSS SREGRRPRFF STTTTSAERP
VDDDEWETVV GLELHVQIGA KTKLFSGAER LYGAEANANV APFDAALPGS LPAVNARAVE
LAARLGFALG ADVQSRSSFD RKHYHYPDLP HGYQITQQRS PIALGGSLDV FVRDGVSGTL
RVERLQLEMD TGKSSKAKSS TLVDLNRAGS TLVEIVTAPD LRGAEEASAA AETFQKVVRF
LGVGDANMEE GSMRVDVNVS HRTRDGAVAG ERCEVKNLNS FRSIARAVAH ERTRQIALLK
RGQRVRRQTR SFDPATGATA VLRDKEALLD YRFAPEPDLP PVVIEPAALR AIKAAVPELP
STAAARLTNT AGLAPKLAQT IASKPSTVAY FDACAEAADA WSTRNGTVTV DKQDVANWVT
GVLVGAVKRA GVTHKGGAGG EPLRGLPESA GAARVGELLA RVAASTSMDS GALEATCAAV
VASMPEQLAA YRGGRTRAMG SFVGEVMKRT KGRADPRRAA EIIKTLVDQ
