Q1IJG7 (SYA_KORVE) 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:	Acid345_3983

Organism

Koribacter versatilis (strain Ellin345)

Taxonomic identifier

204669 [NCBI]

Taxonomic lineage

Bacteria › Acidobacteria › Candidatus Koribacter

Protein attributes

Sequence length	1098 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 By similarity 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 – 1098	1098	Alanine--tRNA ligase HAMAP MF_00036_B		PRO_0000347469
Sites
	Metal binding	779	1	Zinc Potential
	Metal binding	783	1	Zinc Potential
	Metal binding	883	1	Zinc Potential
	Metal binding	887	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	Q1IJG7 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: AD8FFAAA5C9A1D5A	FASTA	1,098	120,722
	10 20 30 40 50 60 MTGRCLIKYS FTPMMTGSQV RRRFLDFFIS KGHKEVHSSS LVPANDPTLL FTNAGMNQFK 70 80 90 100 110 120 DVFLGVEKRD YNRATTSQKC VRAGGKHNDL ENVGFTNRHH TFFEMLGNFS FGDYFKKDAI 130 140 150 160 170 180 AYAWELVTSP DWYGMQQDKL YATIFKGENG VPRDDEAYQL WLDVGVPKER VFEMGMKDNF 190 200 210 220 230 240 WAMGDTGPCG PCSELHYDMG VASSDKKNPE CAAGECKFPC ECGRYVEIWN LVFMQFDRDA 250 260 270 280 290 300 SGTLNPLPKP SIDTGAGLER VTAVMQGVVS NYDTDLFTPL IKRAAELTDV DEKREEAKES 310 320 330 340 350 360 QSKSAASLRV IADHSRAATF LISDGVIPAN EGRGYVLRKI IRRGIRHGRL LGQNKPFLHD 370 380 390 400 410 420 MVYAVRDLMQ DAYPELKETA DRVAKTVLAE ETRFANTLDI GLKKLDEDLA SLAETTRELG 430 440 450 460 470 480 RLSWEEPKPV EFALKEVARH VFVVAQMLSP GMTFDTPGHG FLLRRGIYRA WMDLKAVGLD 490 500 510 520 530 540 RVVRLSEIAE ALSEGETGRV QSVAKNLAHT KQILDAEQER LQSASSQLEF ELDAMEAEKK 550 560 570 580 590 600 LAENPEMLAE QVREVFGPAL EEKVINELRG KLQSRPVYSG DKAFKLYDTF GLPLDFMVDA 610 620 630 640 650 660 ARDQGIEFDQ AGFDAAMESQ RETARASWKG GSKLSASPIY RELAEELGTK PYPGQLAGGH 670 680 690 700 710 720 PMITPQSIFV GYTSTEFKGA TVLAIISNGA SVAQLAPGDV AEMVLDYTPF YSESGGQIGD 730 740 750 760 770 780 TGWLYDSTGN TVVAEVETVQ SPVQGVRAHK VTARQNIAVG DKLNAVVNAD VRRATMRNHT 790 800 810 820 830 840 GTHLLHAALR EVLGKHVKQA GSLVDPAKLR FDFSHFTGVA DEELQDIEDI VNKEVLKNDR 850 860 870 880 890 900 VEVIENVPID VAVNEYKAMA LFGEKYGDRV RVIKIGDFST ELCGGTHTLA TGEIGLIKVL 910 920 930 940 950 960 HEGSVSSGVR RLEAVTGENS VRHFRKDHEL EGVVSTIVRP SEGLSPAQAL KFELDRREEE 970 980 990 1000 1010 1020 IKKLRKELEQ SRMKSASSAV SSATESAREV KGIKVLATRA DNIDRNQMRT LIDNLRSKLG 1030 1040 1050 1060 1070 1080 SGVIVLGSVQ DGKVALIVGV TKDLTSKIQA GKIIAQVAKH VGGSGGGRPD MAEAGGKDPA 1090 ALDGALNATY GIVDSLLS

References

[1]

"Three genomes from the phylum Acidobacteria provide insight into the lifestyles of these microorganisms in soils." Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., Davidsen T.M. , DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R. Appl. Environ. Microbiol. 75:2046-2056(2009) [PubMed: 19201974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ellin345.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000360 Genomic DNA. Translation: ABF42983.1.
RefSeq	YP_593057.1. NC_008009.1.
3D structure databases
ProteinModelPortal	Q1IJG7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1IJG7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4072456.
GenomeReviews	Gene locus Acid345_3983 in contig CP000360_GR.
KEGG	aba:Acid345_3983.
NMPDR	fig|204669.6.peg.3967.
PATRIC	31985252. VBICanKor57425_4251.
Phylogenomic databases
eggNOG	COG0013.
HOGENOM	HBG354397.
OMA	GESKTDQ.
PhylomeDB	Q1IJG7.
Enzyme and pathway databases
BioCyc	ABAC204669:ACID345_3983-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. IPR003156. Pesterase_DHHA1. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
KO	K01872.
PANTHER	PTHR11777:SF6. PTHR11777:SF6. 1 hit.
Pfam	PF02272. DHHA1. 1 hit. PF01411. tRNA-synt_2c. 2 hits. 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. 2 hits. 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_KORVE

Accession

Primary (citable) accession number: Q1IJG7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	June 13, 2006
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program