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Database: UniProt/TrEMBL
Entry: F4L1X9_HALH1
LinkDB: F4L1X9_HALH1
Original site: F4L1X9_HALH1 
ID   F4L1X9_HALH1            Unreviewed;       506 AA.
AC   F4L1X9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   19-FEB-2014, entry version 21.
DE   RecName: Full=Glutamate--tRNA ligase;
DE            EC=6.1.1.17;
DE   AltName: Full=Glutamyl-tRNA synthetase;
GN   Name=gltX; OrderedLocusNames=Halhy_2744;
OS   Haliscomenobacter hydrossis (strain ATCC 27775 / DSM 1100 / LMG 10767
OS   / O).
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Saprospiraceae; Haliscomenobacter.
OX   NCBI_TaxID=760192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27775 / DSM 1100 / LMG 10767 / O;
RX   PubMed=21886862; DOI=10.4056/sigs.1964579;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Daligault H., Lapidus A., Zeytun A., Nolan M., Lucas S., Del Rio T.G.,
RA   Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Ivanova N., Huntemann M., Mavromatis K.,
RA   Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Brambilla E.M., Rohde M., Verbarg S., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Woyke T.;
RT   "Complete genome sequence of Haliscomenobacter hydrossis type strain
RT   (O).";
RL   Stand. Genomic Sci. 4:352-360(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 1100;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA   Pagani I., Daligault H., Detter J.C., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Verbarg S.,
RA   Frueling A., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "Complete sequence of chromosome of Haliscomenobacter hydrossis DSM
RT   1100.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a
CC       two-step reaction: glutamate is first activated by ATP to form
CC       Glu-AMP and then transferred to the acceptor end of tRNA(Glu) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP +
CC       diphosphate + L-glutamyl-tRNA(Glu).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP002691; AEE50612.1; -; Genomic_DNA.
DR   RefSeq; YP_004447485.1; NC_015510.1.
DR   ProteinModelPortal; F4L1X9; -.
DR   EnsemblBacteria; AEE50612; AEE50612; Halhy_2744.
DR   GeneID; 10586916; -.
DR   KEGG; hhy:Halhy_2744; -.
DR   PATRIC; 54602206; VBIHalHyd147579_2948.
DR   KO; K01885; -.
DR   OMA; RANQGKF; -.
DR   BioCyc; HHYD760192:GI21-2766-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 1.10.1160.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_00022_B; Glu_tRNA_synth_B; 1.
DR   InterPro; IPR008925; aa-tRNA-synth_I_codon-bd.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR10119; PTHR10119; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF48163; SSF48163; 1.
DR   TIGRFAMs; TIGR00464; gltX_bact; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   MOTIF        10     20       "HIGH" region (By similarity).
FT   MOTIF       257    261       "KMSKS" region (By similarity).
FT   BINDING     260    260       ATP (By similarity).
SQ   SEQUENCE   506 AA;  57558 MW;  A21F63B4D2301367 CRC64;
     MENIRVRFAP SPTGALHIGG IRTALYNYLL AKKFGGTFIL RIEDTDQTRY VPGAEAYIIE
     SLRWAGIVPM EGPGFGGAYG PYRQSDRKEI YLEYAQQLVD NGHGYYAFDT PEELDAVRKA
     DENFKYDSKT RLKLKNSLTL SAEEVKRRLN AEEPYVIRLK VPEDQSILIQ DLVRDEVSFQ
     SNELDDKVML KGDGMPTYHL ANVIDDRLMK ITHVIRGEEW LPSTAHHVLL YRAFGWETEM
     PRFAHLPLIL KPDGKGKLSK RDGFRLGIPV FPISWNGETP EDSFIGFREF GFDPRAMVNF
     MAFMGWNPGT EQEIFSMDEL AEAFTVEKIG KSGARFDFDK AKWFNQQYIM ATPDAALAKT
     VRPIIEAHGH QPAEDFLRSF VGMMKERVIL FPDFWTNGAY FFEDFTVFDE ATIRKKWKAE
     GSRVIFAPLV EQLEALSDYT ATTVQTCVEA FTANAGLKFG DVLPILRVGL TGTMKGPAVF
     DMMALLGKAE CRRRLERAFD LFDKVS
//
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