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Database: UniProt/SWISS-PROT
Entry: GATB_NEIMF
LinkDB: GATB_NEIMF
Original site: GATB_NEIMF 
ID   GATB_NEIMF              Reviewed;         476 AA.
AC   A1KUI0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-OCT-2019, entry version 74.
DE   RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B {ECO:0000255|HAMAP-Rule:MF_00121};
DE            Short=Asp/Glu-ADT subunit B {ECO:0000255|HAMAP-Rule:MF_00121};
DE            EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00121};
GN   Name=gatB {ECO:0000255|HAMAP-Rule:MF_00121};
GN   OrderedLocusNames=NMC1293;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 /
OS   DSM 15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C.,
RA   Arrowsmith C., Chillingworth T., Cronin A., Davis P.H., Holroyd N.E.,
RA   Jagels K., Maddison M., Moule S., Rabbinowitsch E., Sharp S.,
RA   Unwin L., Whitehead S., Quail M.A., Achtman M., Barrell B.G.,
RA   Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
CC   -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn)
CC       or Gln-tRNA(Gln) through the transamidation of misacylated Asp-
CC       tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both
CC       of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction
CC       takes place in the presence of glutamine and ATP through an
CC       activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
CC       {ECO:0000255|HAMAP-Rule:MF_00121}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP +
CC         H(+) + 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_00121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2
CC         H(+) + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:14513, Rhea:RHEA-COMP:9674, Rhea:RHEA-COMP:9677,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78515, ChEBI:CHEBI:78516, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00121};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_00121}.
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00121}.
DR   EMBL; AM421808; CAM10523.1; -; Genomic_DNA.
DR   RefSeq; WP_002220838.1; NC_008767.1.
DR   SMR; A1KUI0; -.
DR   PRIDE; A1KUI0; -.
DR   EnsemblBacteria; CAM10523; CAM10523; NMC1293.
DR   KEGG; nmc:NMC1293; -.
DR   HOGENOM; HOG000223743; -.
DR   KO; K02434; -.
DR   OMA; ARKWWMG; -.
DR   OrthoDB; 497127at2; -.
DR   BioCyc; NMEN272831:G1G1U-1483-MONOMER; -.
DR   Proteomes; UP000002286; Chromosome.
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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.410; -; 1.
DR   Gene3D; 1.10.150.380; -; 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; IPR042114; GatB_C_1.
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; Complete proteome; Ligase; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN         1    476       Aspartyl/glutamyl-tRNA(Asn/Gln)
FT                                amidotransferase subunit B.
FT                                /FTId=PRO_1000016007.
SQ   SEQUENCE   476 AA;  51678 MW;  A4D519F269726A27 CRC64;
     MTWETVIGLE IHVQLNTKSK IFSGASTAFG AEPNAHASVV ECALPGVLPV MNREVVEKAI
     KLGLALDAKI NRKNVFDRKN YFYPDLPKGY QISQLDLPIV EHGKLEIVVG DDVKTINVTR
     AHMEEDAGKS VHEGLNGATG IDLNRAGTPL LEVVSEPELR SAAEAVAYAK ALHSLVTWLD
     ICDGNMAEGS FRVDANVSVR PKGQAEFGTR REIKNLNSFR FLEQAINYEA EAQIEILEDG
     SKVQQATMLF DPEKGETRVM RLKEDAQDYR YFPDPDLLPV IISDAQMQKA KAEMPELPKE
     MAARFVADYG VSEYDARLLT ASRAQAAYFE EAAKASGQGK PTANWMNGEL AAALNKAGLE
     LADSPITAPR LAALVGKIAD GTLSSKLAKK AFEAMWAEPE STIAEIIEKH GLQQMTDTGA
     VEAMVDEVLA NNAKAVEQFK SGNEKALNAI VGQVMKASKG KANPAQVQEL IKAKLA
//
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