Q8A0M6 (SYA_BACTN) 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:	BT_3995

Organism

Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)

Taxonomic identifier

226186 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length	872 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 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 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 – 872	872	Alanine--tRNA ligase HAMAP MF_00036_B		PRO_0000075061
Sites
	Metal binding	563	1	Zinc Potential
	Metal binding	567	1	Zinc Potential
	Metal binding	665	1	Zinc Potential
	Metal binding	669	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8A0M6 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: DA62252A4928E842	FASTA	872	97,554
	10 20 30 40 50 60 MLTAKEIRDS FKNFFESKGH HIVPSAPMVI KDDPTLMFTN AGMNQFKDII LGNHPAKYHR 70 80 90 100 110 120 VADSQKCLRV SGKHNDLEEV GHDTYHHTMF EMLGNWSFGD YFKKEAINWA WEYLVEVLKL 130 140 150 160 170 180 NPEHLYATVF EGSPEEGLSR DDEAASYWEQ YLPKDHIING NKHDNFWEMG DTGPCGPCSE 190 200 210 220 230 240 IHIDLRPAEE RAKISGRDLV NHDHPQVIEI WNLVFMQYNR KADGSLEPLP AKVIDTGMGF 250 260 270 280 290 300 ERLCMALQGK TSNYDTDVFQ PMLKAIAAMS GTEYGKDKQQ DIAMRVIADH IRTIAFSITD 310 320 330 340 350 360 GQLPSNAKAG YVIRRILRRA VRYGYTFLGQ KQSFMYKLLP VLIDNMGDAY PELIAQKGLI 370 380 390 400 410 420 EKVIKEEEEA FLRTLETGIR LLDKTMGDTK AAGKTEISGK DAFTLYDTFG FPLDLTELIL 430 440 450 460 470 480 RENGMTVNIE EFNAEMQQQK QRARNAAAIE TGDWVTLREG TTEFVGYDYT EYEASILRYR 490 500 510 520 530 540 QIKQKNQTLY QIVLDCTPFY AESGGQVGDT GVLVSEFETI EVIDTKKENN LPIHITKKLP 550 560 570 580 590 600 EHPEAPMMAC VDTDKRAACA ANHSATHLLD SALREVLGEH IEQKGSLVTP DSLRFDFSHF 610 620 630 640 650 660 QKVTDEEIRQ VEHLVNAKIR ANIPLKEYRN IPIEEAKELG AIALFGEKYG ERVRVIQFGS 670 680 690 700 710 720 SIEFCGGIHV AATGNIGMVK IISESSVAAG VRRIEAYTGA RVEEMLDTIQ DTISELKSLF 730 740 750 760 770 780 NNAPDLGIAI RKYIEENAGL KKQVEDYMKE KEASLKERLL KNIQEIHGIK VIKFCAPLPA 790 800 810 820 830 840 EVVKNIAFQL RGEITENLFF VAGSLDNGKP MLTVMLSDNL VAGGLKAGNL VKEAAKLIQG 850 860 870 GGGGQPHFAT AGGKNTDGLN AAIEKVLELA GI

References

[1]

"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis." Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I. Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE015928 Genomic DNA. Translation: AAO79100.1.
RefSeq	NP_812906.1. NC_004663.1.
3D structure databases
ProteinModelPortal	Q8A0M6.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1073082.
GenomeReviews	Gene locus BT_3995 in contig AE015928_GR.
KEGG	bth:BT_3995.
NMPDR	fig|226186.1.peg.3993.
PATRIC	21063026. VBIBacThe70966_4061.
Phylogenomic databases
HOGENOM	HBG354397.
OMA	VILEMES.
PhylomeDB	Q8A0M6.
ProtClustDB	PRK00252.
Enzyme and pathway databases
BioCyc	BTHE226186:BT_3995-MONOMER.
Family and domain databases
HAMAP	MF_00036_B. Ala_tRNA_synth_B. [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. IPR003156. Pesterase_DHHA1. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
KO	K01872.
Pfam	PF02272. DHHA1. 1 hit. 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.
TIGRFAMs	TIGR00344. AlaS. 1 hit.
PROSITE	PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYA_BACTN

Accession

Primary (citable) accession number: Q8A0M6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program