ID F4L1X9_HALH1 Unreviewed; 506 AA.
AC F4L1X9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 29-MAY-2013, entry version 19.
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 BioCyc; HHYD760192:GI21-2766-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA: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_Ib_bac/mito.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth_Ib.
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 PANTHER; PTHR10119:SF1; PTHR10119:SF1; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF48163; tRNA-synt_bind; 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
//
