O51238 (SYA_BORBU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	BB_0220

Organism

Borrelia burgdorferi (Lyme disease spirochete)

Taxonomic identifier

139 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length	594 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 MF_00036_B
Catalytic activity	ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_B
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_B
Subcellular location	Cytoplasm HAMAP MF_00036_B.
Domain	Consists of two domains; the N-terminal catalytic domain (in this organism this is shorter than usual) and the editing domain; the C-terminal C-Ala domain found in most orthologs is missing. The editing domain removes incorrectly charged amino acids By similarity. HAMAP MF_00036_B
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	alanyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW alanine-tRNA ligase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 594	594	Alanine--tRNA ligase HAMAP MF_00036_B		PRO_0000075072
Sites
	Metal binding	456	1	Zinc Potential
	Metal binding	460	1	Zinc Potential
	Metal binding	558	1	Zinc Potential
	Metal binding	562	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	O51238 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 2337B306FD02349A	FASTA	594	67,773
	10 20 30 40 50 60 MTLNKLRKKY IDFFKSKKHF EIMGKSLVPE NDPTVLFNTA GMQPLIPYLL GEVHPSGDML 70 80 90 100 110 120 VNVQKCLRTG DIDEVGDLSH LTFFEMLGNW SLGAYFKEYS VKCSFEFLTS SDYLNIPKDS 130 140 150 160 170 180 LYVSVFEGDQ EIPRDTETAK VWESLGISKD RIHYLSKDHN FWGPVGSKGP CGPDTEIYVD 190 200 210 220 230 240 TGKSKCSLDC NITCSCGKYF EIWNNVFMQY NKDENGNYIE LGRKCVDTGM GLERTIAFLQ 250 260 270 280 290 300 GKSSVYDTDA FMPIIKRIEY ISGKIYGQKE DDDRCIRIIS DHVKAACFIL ADSSVVFPSN 310 320 330 340 350 360 LGQGYVLRRL IRRSIRYAKK LGIKSHFLAD LVDSVEAIYR SFYNELTEKK DFIKKELSKE 370 380 390 400 410 420 EEKFFKTLSQ GEQEFIKITR NLPSKTIPGD IAFKLYDTYG FPYEVTEELA IEYGFNVDKL 430 440 450 460 470 480 GFNEHFKKHQ KTSKKGGDKV FKGGLADYTY ETTKLHTATH LLHKALQLVL GDHVRQKGSN 490 500 510 520 530 540 ITAERLRFDF VHSEKMTDDE IKKVEEIVNL QIKNSLSVKK IIMELSEARE KGAMALFGEK 550 560 570 580 590 YDDLVSVYEI DGFSLEVCGG PHVENTNELG TFKIQKEQSS SSGIRRIKAI LIDE

References

[1]

"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C. Nature 390:580-586(1997) [PubMed: 9403685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000783 Genomic DNA. Translation: AAC66604.1.
PIR	D70127.
RefSeq	NP_212354.1. NC_001318.1.
3D structure databases
ProteinModelPortal	O51238.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBORT00000008876; EBBORP00000008206; EBBORG00000008875.
GeneID	1195057.
GenomeReviews	Gene locus BB_0220 in contig AE000783_GR.
KEGG	bbu:BB0220.
NMPDR	fig|224326.1.peg.604.
PATRIC	20557054. VBIBorBur75917_0618.
TIGR	BB_0220.
Phylogenomic databases
GeneTree	EBGT00050000006849.
HOGENOM	HBG354397.
OMA	RKCVDTG.
ProtClustDB	PRK01584.
Enzyme and pathway databases
BioCyc	BBUR224326:BB_0220-MONOMER.
Family and domain databases
HAMAP	MF_00036_B. Ala_tRNA_synth_B. Divergent sequence. [Tree]
InterPro	IPR002318. Ala-tRNA-synth_IIc. IPR018162. Ala-tRNA-synth_IIc_anticod-bd. IPR018165. Ala-tRNA-synth_IIc_core. IPR018164. Ala-tRNA-synth_IIc_N. IPR023033. Ala_tRNA_synth_euk/bac. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
KO	K01872.
PANTHER	PTHR11777:SF6. PTHR11777:SF6. 1 hit.
Pfam	PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view]
PRINTS	PR00980. TRNASYNTHALA.
SMART	SM00863. tRNA_SAD. 1 hit. [Graphical view]
SUPFAM	SSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit. SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
PROSITE	PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYA_BORBU

Accession

Primary (citable) accession number: O51238

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	June 1, 1998
Last modified:	January 25, 2012
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program