Q9XDM3 (SYA_AQUPY) 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

Organism

Aquifex pyrophilus

Taxonomic identifier

2714 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	871 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
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 – 871	871	Alanine--tRNA ligase HAMAP MF_00036_B		PRO_0000075048
Sites
	Metal binding	559	1	Zinc Potential
	Metal binding	563	1	Zinc Potential
	Metal binding	661	1	Zinc Potential
	Metal binding	665	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9XDM3 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: D2D15915FC00CC31	FASTA	871	99,395
	10 20 30 40 50 60 MGFSAHEIRE LFLSFFEKKG HTRVKSAPLV PENDPTLLFV NAGMVPFKNV FLGLEKRPYK 70 80 90 100 110 120 RATSCQKCLR VSGKHNDLEQ VGYTSRHHTF FEMLGNFSFG DYFKKEAIEY AWEFVTEVLK 130 140 150 160 170 180 LPKERLYVSV YKDDEEAYRI WNEHIGIPSE RIWRLGEEDN FWQMGDTGPC GPSSEIYVDR 190 200 210 220 230 240 GEEYEGEERY LEIWNLVFMQ YNRDENGVLT PLPHPNIDTG MGLERIASVL QGKNSNFEID 250 260 270 280 290 300 IIYPLIEFGE EVSGKKYGEK FETDVALRVI ADHLRAITFA ISDGVIPSNE GRGYVIRRIL 310 320 330 340 350 360 RRAMRFGYQL GITEPFLYKG IDLVVDIMKE PYPELELSRD FVKGIVKGEE ERFIRTLRSG 370 380 390 400 410 420 MEYIQEVIEK ALSEGRKTLT GKEVFTAYDT YGFPVDLIQE IAKEKGLEID LEGFQCELEE 430 440 450 460 470 480 QRERARKSFK IETKEVKPVY AHLKELGITS RFVGYEHLEY ETEVLGIIVG DEIVSEIKEG 490 500 510 520 530 540 EEGEIILRET PFYPEGGGQI GDSGIIETDK GIFKVEDTQR PTEGIIVHIG KLLKGKISVK 550 560 570 580 590 600 DIVHARVDKE RRWDIMRNHT ATHLLHAALR NLLGEHVRQA GSLVADKYLR FDFTHFSPLT 610 620 630 640 650 660 EEEIKRIEEL VNEKIRENLP VSVMEMAYQE ALQTGAIAIF EEKYGERVRV ISCGEFSKEL 670 680 690 700 710 720 CGGTHVSATG DIGYFKIISE SSVGAGVRRI VAQTGRWAVN TAFEEHTTLK KVSNALGVKE 730 740 750 760 770 780 DEVVQKVEEL KEEIKEKEKE IQKLRQEILK LQIREKVKEE RHRELTLYYG VFEDVEPEEL 790 800 810 820 830 840 RNLADILRQR TGKDVVFIAS KKEGKINFVI ASSKGISKEV RANELIRQVG KVLKGGGGGR 850 860 870 EDLAQGGGKA PDKFDESVKL LKELLSGVSV G

References

[1]

"RNA polymerase of Aquifex pyrophilus: implications for the evolution of the bacterial rpoBC operon and extremely thermophilic bacteria." Klenk H.-P., Meier T.D., Durovic P., Schwass V., Lottspeich F., Dennis P.P., Zillig W. J. Mol. Evol. 48:528-541(1999) [PubMed: 10198119] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Kol5A / DSM 6858 / JCM 9492.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF027500 Genomic DNA. Translation: AAD25871.1.
3D structure databases
ProteinModelPortal	Q9XDM3.
SMR	Q9XDM3. Positions 3-454.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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]
PANTHER	PTHR11777:SF6. PTHR11777:SF6. 1 hit.
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_AQUPY

Accession

Primary (citable) accession number: Q9XDM3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program