GATB1_MICPC
ID GATB1_MICPC Reviewed; 545 AA.
AC C1MIE8;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B-1, chloroplastic/mitochondrial;
DE Short=Glu-AdT subunit B-1 {ECO:0000255|HAMAP-Rule:MF_03147};
DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_03147};
GN Name=GATB-1 {ECO:0000255|HAMAP-Rule:MF_03147}; ORFNames=MICPUCDRAFT_50541;
OS Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Mamiellaceae; Micromonas.
OX NCBI_TaxID=564608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1545;
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; GG663735; EEH60907.1; -; Genomic_DNA.
DR RefSeq; XP_003055655.1; XM_003055609.1.
DR AlphaFoldDB; C1MIE8; -.
DR SMR; C1MIE8; -.
DR STRING; 564608.C1MIE8; -.
DR GeneID; 9680990; -.
DR KEGG; mpp:MICPUCDRAFT_50541; -.
DR eggNOG; KOG2438; Eukaryota.
DR OMA; ARKWWMG; -.
DR OrthoDB; 898782at2759; -.
DR Proteomes; UP000001876; Unassembled WGS sequence.
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; 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; Chloroplast; Ligase; Mitochondrion; Nucleotide-binding;
KW Plastid; Protein biosynthesis; Reference proteome.
FT CHAIN 1..545
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit B-1,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000413225"
SQ SEQUENCE 545 AA; 58917 MW; 8F8864E4D48D22EE CRC64;
MAHACARGVV APAPSRVSPR VSGRRVVVAR VGTSSAEASA KEAPKKSEAK GANEVQFEAV
IGIETHVQIN SNTKAFCRCA AVYGAEPNRH TCPVCLGHPG TYPILNAAVV KKAIALGIGL
DCSVIRRKST FDRKQYFYPD LPKGYQISQF DEPYGEHGKL DVVIPVEDGG GVRTIGITRA
HIEEDAGKLT HFPAKGNEPG YALADYNRAG VALVEIVSEP DLRTGREVAA YGAELRRLVR
YLDVSDGNLS EGSMRCDVNV SVRPVGREAF GTKVEVKNMN SFNAMSRAVD FEIERQTTLI
RDGRGDEIVQ ETRTWDEGRQ RTVSMRKKEG LADYRYFPEP DLPPLVFDNA YVDGVKAEMP
ELPAAIRARY AALGLPDDAV QVLVEDKALV EYFDATIAAG APAKQAANWL TGDIMAYLKN
AKDVTISTMP LRSKDLAEFC SMIENGEISG KIGKDILPDL LVGETGGAGP RAIVEERGLS
QISDPAEIEA IVDKVLEENP GQLEQYRGGK DKLKGFFVGK VLAASGGRAN PALSNQILMK
KLAGE
