Alanyl-tRNA synthetase - Escherichia coli (strain K12)

Contribute

Send feedback

Reviewed, UniProtKB/Swiss-Prot P00957 (SYA_ECOLI)

Last modified November 25, 2008. Version 94. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Alanyl-tRNA synthetase
    EC=6.1.1.7
Alternative name(s):
    Alanine--tRNA ligase
      Short name=AlaRS

Gene names

Name:	alaS
Synonyms:	lovB
Ordered Locus Names:	b2697, JW2667

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Hide | Top

Protein attributes

Sequence length	876 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity	ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).
Cofactor	Binds 1 zinc ion per subunit.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Hide | Top

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Domain	Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	alanyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	mitochondrion Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP alanine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP nucleic acid binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 876

876

Alanyl-tRNA synthetase

PRO_0000075113

Regions

Zinc finger

179 – 192

C2H2-type

Region

1 – 461

461

Catalytic

Region

699 – 808

110

Important for oligomerization

Amino acid modifications

Modified residue

N6-acetyllysine

Experimental info

Mutagenesis

179

C → S: Inactivates the enzyme

Mutagenesis

182

C → S: No inactivation

Mutagenesis

184

E → Q: No inactivation

Mutagenesis

188

D → N: No inactivation

Mutagenesis

189

H → Q: Inactivates the enzyme

Mutagenesis

191

D → N: No inactivation

Mutagenesis

192

H → Q: Inactivates the enzyme

Sequence conflict

29 – 33

LVPHN → RYHIT Ref.4 Ref.5

Sequence conflict

158

G → N Ref.4 Ref.5

Sequence conflict

168

D → G in AAA03208. Ref.5

Sequence conflict

172

Q → R in AAA03208. Ref.5

Sequence conflict

175

D → G in AAA03208. Ref.5

Sequence conflict

180

G → D in AAA03208. Ref.5

Sequence conflict

584

Q → H in AAA03208. Ref.5

Sequence conflict

619

Q → L in AAA03208. Ref.5

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P00957-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 73F69C69FCF8C08C
Show »

FASTA

876

96,032

        10         20         30         40         50         60 
MSKSTAEIRQ AFLDFFHSKG HQVVASSSLV PHNDPTLLFT NAGMNQFKDV FLGLDKRNYS 

        70         80         90        100        110        120 
RATTSQRCVR AGGKHNDLEN VGYTARHHTF FEMLGNFSFG DYFKHDAIQF AWELLTSEKW 

       130        140        150        160        170        180 
FALPKERLWV TVYESDDEAY EIWEKEVGIP RERIIRIGDN KGAPYASDNF WQMGDTGPCG 

       190        200        210        220        230        240 
PCTEIFYDHG DHIWGGPPGS PEEDGDRYIE IWNIVFMQFN RQADGTMEPL PKPSVDTGMG 

       250        260        270        280        290        300 
LERIAAVLQH VNSNYDIDLF RTLIQAVAKV TGATDLSNKS LRVIADHIRS CAFLIADGVM 

       310        320        330        340        350        360 
PSNENRGYVL RRIIRRAVRH GNMLGAKETF FYKLVGPLID VMGSAGEDLK RQQAQVEQVL 

       370        380        390        400        410        420 
KTEEEQFART LERGLALLDE ELAKLSGDTL DGETAFRLYD TYGFPVDLTA DVCRERNIKV 

       430        440        450        460        470        480 
DEAGFEAAME EQRRRAREAS GFGADYNAMI RVDSASEFKG YDHLELNGKV TALFVDGKAV 

       490        500        510        520        530        540 
DAINAGQEAV VVLDQTPFYA ESGGQVGDKG ELKGANFSFA VEDTQKYGQA IGHIGKLAAG 

       550        560        570        580        590        600 
SLKVGDAVQA DVDEARRARI RLNHSATHLM HAALRQVLGT HVSQKGSLVN DKVLRFDFSH 

       610        620        630        640        650        660 
NEAMKPEEIR AVEDLVNTQI RRNLPIETNI MDLEAAKAKG AMALFGEKYD ERVRVLSMGD 

       670        680        690        700        710        720 
FSTELCGGTH ASRTGDIGLF RIISESGTAA GVRRIEAVTG EGAIATVHAD SDRLSEVAHL 

       730        740        750        760        770        780 
LKGDSNNLAD KVRSVLERTR QLEKELQQLK EQAAAQESAN LSSKAIDVNG VKLLVSELSG 

       790        800        810        820        830        840 
VEPKMLRTMV DDLKNQLGST IIVLATVVEG KVSLIAGVSK DVTDRVKAGE LIGMVAQQVG 

       850        860        870 
GKGGGRPDMA QAGGTDAAAL PAALASVKGW VSAKLQ

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Mass spectra of partial protein hydrolysates as a multiple phase check for long polypeptides deduced from DNA sequences: NH2-terminal segment of alanine tRNA synthetase." Herlihy W.C., Royal N.J., Biemann K., Putney S.D., Schimmel P.R. Proc. Natl. Acad. Sci. U.S.A. 77:6531-6535(1980) [PubMed: 7005898] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-166, PARTIAL PROTEIN SEQUENCE.
[5]	"Primary structure of a large aminoacyl-tRNA synthetase." Putney S.D., Royal N.J., de Vegvar H.N., Herlihy W.C., Biemann K., Schimmel P. Science 213:1497-1501(1981) [PubMed: 7025207] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-876.
[6]	"Acceptor helix interactions in a class II tRNA synthetase: photoaffinity cross-linking of an RNA miniduplex substrate." Musier-Forsyth K., Schimmel P. Biochemistry 33:773-779(1994) [PubMed: 8292605] [Abstract] Cited for: PROTEIN SEQUENCE OF 163-173.
[7]	"Evidence for involvement of Escherichia coli genes pmbA, csrA and a previously unrecognized gene tldD, in the control of DNA gyrase by letD (ccdB) of sex factor F." Murayama N., Shimizu H., Takiguchi S., Baba Y., Amino H., Horiuchi T., Sekimizu K., Miki T. J. Mol. Biol. 256:483-502(1996) [PubMed: 8604133] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 799-876. Strain: KP4714.
[8]	"Identification and molecular characterization of csrA, a pleiotropic gene from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis, cell size, and surface properties." Romeo T., Gong M., Liu M.-Y., Brun-Zinkernagel A.-M. J. Bacteriol. 175:4744-4755(1993) [PubMed: 8393005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 866-876. Strain: K12.
[9]	"Cloning, partial sequencing, and in vitro transcription of the gene for alanine tRNA synthetase." Putney S.D., Melendez D.L., Schimmel P.R. J. Biol. Chem. 256:205-211(1981) [PubMed: 6256345] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
[10]	"Evidence for a 'cysteine-histidine box' metal-binding site in an Escherichia coli aminoacyl-tRNA synthetase." Miller W.T., Hill K.A.W., Schimmel P. Biochemistry 30:6970-6976(1991) [PubMed: 1712632] [Abstract] Cited for: ZINC-BINDING.
[11]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in E. coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 0:0-0(2008) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74, MASS SPECTROMETRY.

Hide | Top

Cross-references

Sequence databases
	U00096 Genomic DNA. Translation: AAC75739.1. AP009048 Genomic DNA. Translation: BAA16559.1. J01581 Unassigned DNA. Translation: AAA03208.1. L07596 Unassigned DNA. Translation: AAA71918.1. Sequence problems. D44453 Genomic DNA. Translation: BAA21554.1. Z28405 Genomic DNA. Translation: CAA82247.1.
PIR	SYECAT. E65049.
RefSeq	AP_003264.1. NP_417177.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:9080N.
2-D gel databases
SWISS-2DPAGE	P00957.
ECO2DBASE	F093.0. 6TH EDITION.
Genome annotation databases
GeneID	947175.
GenomeReviews	Gene locus b2697 in contig U00096_GR. Gene locus JW2667 in contig AP009048_GR.
KEGG	ecj:JW2667. eco:b2697.
Organism-specific databases
EchoBASE	EB0033.
EcoGene	EG10034. alaS.
CMR	Search...
Phylogenomic databases
HOGENOM	P00957.
Enzyme and pathway databases
BioCyc	EcoCyc:ALAS-MON. MetaCyc:ALAS-MON.
Family and domain databases
HAMAP	MF_00036. [Tree]
InterPro	IPR002318. Ala-tRNA-synth_IIc. IPR003156. Pesterase_DHHA1. IPR012947. tRNA_SAD. [Graphical view]
Pfam	PF02272. DHHA1. 1 hit. PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view]
PRINTS	PR00980. TRNASYNTHALA.
TIGRFAMs	TIGR00344. alaS. 1 hit.
PROSITE	PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view]
ProtoNet	Search...

Hide | Top

Entry information

Entry name

SYA_ECOLI

Accession

Primary (citable) accession number: P00957
Secondary accession number(s): P78279

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 1997
Last modified:	November 25, 2008
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents