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O67323 (SYA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alanine--tRNA ligase
EC=6.1.1.7
Alternative name(s):
Alanyl-tRNA synthetase
Short name=AlaRS
Gene names
Name:alaS
Ordered Locus Names:aq_1293
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex ›

Protein attributes

Sequence length867 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain By similarity. HAMAP-Rule MF_00036

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP-Rule MF_00036

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Cytoplasm HAMAP-Rule MF_00036.

Domain

Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs. The Aquifex aeolicus domain can be used in vitro to replace the corresponding domain in E.coli. Ref.3

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 867867Alanine--tRNA ligase HAMAP-Rule MF_00036
PRO_0000075047

Sites

Metal binding5591Zinc Potential
Metal binding5631Zinc Potential
Metal binding6611Zinc Potential
Metal binding6651Zinc Potential

Secondary structure

1 ........................................................................................... 867
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O67323 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: E38C6D376643A149

FASTA86798,436
        10         20         30         40         50         60 
MSLSAHEIRE LFLSFFEKKG HTRVKSAPLV PENDPTLLFV NAGMVPFKNV FLGLEKRPYK 

        70         80         90        100        110        120 
RATSCQKCLR VSGKHNDLEQ VGYTSRHHTF FEMLGNFSFG DYFKKEAIEY AWEFVTEVLK 

       130        140        150        160        170        180 
LPKEKLYVSV YKDDEEAYRI WNEHIGIPSE RIWRLGEEDN FWQMGDVGPC GPSSEIYVDR 

       190        200        210        220        230        240 
GEEYEGDERY LEIWNLVFMQ YNRDENGVLT PLPHPNIDTG MGLERIASVL QGKNSNFEID 

       250        260        270        280        290        300 
IIFPLIQFGE EVSGKKYGEK FETDVALRVI ADHLRAITFA ISDGVIPSNE GRGYVIRRIL 

       310        320        330        340        350        360 
RRAMRFGYKL GIENPFLYKG VDLVVDIMKE PYPELELSRE FVKGIVKGEE KRFIKTLKAG 

       370        380        390        400        410        420 
MEYIQEVIQK ALEEGRKTLS GKEVFTAYDT YGFPVDLIDE IAREKGLGID LEGFQCELEE 

       430        440        450        460        470        480 
QRERARKHFK VEAKKVKPVY SHLKELGKTS AFVGYEHMEW ESQVVGLVKG EGLVSELKEG 

       490        500        510        520        530        540 
EEGEVVLKET PFYPEGGGQI GDAGIIESDK ALFKVEDTQK PTEGIIVHIG KVLKGTLKVG 

       550        560        570        580        590        600 
DTVHARVDKE RRWDIMRNHT ATHLLHAALR NVLGEHVRQA GSLVADKYLR FDFTHFSALT 

       610        620        630        640        650        660 
EEELKRVEEL VNEKIRENLP VNVMEMAYDE ALKTGAIAIF EEKYGERVRV ISCGEFSKEL 

       670        680        690        700        710        720 
CGGTHVSATG DIGYFKIISE SSVGAGVRRI VAQTGRWSVE TAFKEHQTLK KASSALGVGE 

       730        740        750        760        770        780 
EEVIQKIEEL KEEIKDRERE IQRLKQELLK LQIREVVKEE NVGDFTLHYG VFEEVEPEEL 

       790        800        810        820        830        840 
RNLADMLRQR TKKDVVFIAS RKGDKINFVI GVSKEISDKV NAKEVIREVG KVLKGGGGGR 

       850        860 
ADLAQGGGKA PDKFPEAVKL LKEILSG

« Hide

References

« Hide 'large scale' references
[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
[2]"Breaking sieve for steric exclusion of a noncognate amino acid from active site of a tRNA synthetase."
Swairjo M.A., Schimmel P.R.
Proc. Natl. Acad. Sci. U.S.A. 102:988-993(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 1-454 WITH SUBSTRATES OR WITH ATP.
[3]"The C-Ala domain brings together editing and aminoacylation functions on one tRNA."
Guo M., Chong Y.E., Beebe K., Shapiro R., Yang X.-L., Schimmel P.
Science 325:744-747(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN EXCHANGE EXPERIMENTS, X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 758-867.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000657 Genomic DNA. Translation: AAC07289.1.
PIRH70411.
RefSeqNP_213887.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RIQX-ray2.14A1-454[»]
1YFRX-ray2.15A/B1-454[»]
1YFSX-ray2.08A/B1-454[»]
1YFTX-ray2.23A1-454[»]
1YGBX-ray2.48A1-454[»]
3G98X-ray1.85A/B758-867[»]
3HTZX-ray2.50A2-454[»]
ProteinModelPortalO67323.
SMRO67323. Positions 2-454.
ModBaseSearch...

Protein-protein interaction databases

STRING224324.aq_1293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC07289; AAC07289; aq_1293.
GeneID1192761.
KEGGaae:aq_1293.
PATRIC20959788. VBIAquAeo85532_1011.

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHOG000156965.
KOK01872.
OMAEWFDFPK.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-925-MONOMER.

Family and domain databases

HAMAPMF_00036_B. Ala_tRNA_synth_B.
InterProIPR002318. Ala-tRNA-lgiase_IIc.
IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR023033. Ala_tRNA_ligase_euk/bac.
IPR003156. Pesterase_DHHA1.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
PANTHERPTHR11777:SF6. PTHR11777:SF6. 1 hit.
PfamPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR00980. TRNASYNTHALA.
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMSSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit.
SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMsTIGR00344. alaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO67323.

Entry information

Entry nameSYA_AQUAE
AccessionPrimary (citable) accession number: O67323
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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