A9KMW7 (SYA1_CLOPH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alanine--tRNA ligase 1
EC=6.1.1.7

Alternative name(s):
Alanyl-tRNA synthetase 1
Short name=AlaRS 1

Gene names

Name:	alaS1
Ordered Locus Names:	Cphy_2617

Organism

Clostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) [Complete proteome] [HAMAP]

Taxonomic identifier

357809 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	879 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
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 – 879	879	Alanine--tRNA ligase 1 HAMAP MF_00036_B		PRO_0000347571
Sites
	Metal binding	566	1	Zinc Potential
	Metal binding	570	1	Zinc Potential
	Metal binding	668	1	Zinc Potential
	Metal binding	672	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	A9KMW7 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 0D15710A4B7B7E7E	FASTA	879	96,593
	10 20 30 40 50 60 MKVYGVNELR KMYLDFFESK GHLKLNSFSL VPQNDKSLLL INSGMAPLKP YFTGQEIPPK 70 80 90 100 110 120 KRVTTCQKCI RTGDIENIGK TARHGTFFEM LGNFSFGDYF KHEAIAWSWE FLTEVVGLSG 130 140 150 160 170 180 DRLYPSIYLE DDEAFDIWNK EVGIAPERIF RMGKADNFWE HGAGPCGPCS EIYYDRGEKY 190 200 210 220 230 240 GCGDPNCTVG CECDRFIEVW NNVFTQFNSD GNGNYEELEN KNIDTGMGLE RLAVVVQDVD 250 260 270 280 290 300 TLFDIDTMKA IRDHVCKMAN AEYKVDPKKD MSIRLITDHI RSVTFMTSDG IIPSNEGRGY 310 320 330 340 350 360 VLRRLLRRAA RHGRLLGIQG KFLAELSKTV IAESKDGYPE LEEKKEYILK VLTIEEEKFN 370 380 390 400 410 420 KTIDQGLSIL SEMEEALVSN GTKTLNGEDA FKLYDTYGFP LDLTKEILEE KGFSIDEEGF 430 440 450 460 470 480 KKAMQVQRET ARSARAVTNY MGADASIYDE IDPAITSNFV GYDRTSHTSK ISVLTTETDL 490 500 510 520 530 540 TDEVVGGQTA TIIVDETPFY ATMGGQTADI GFIVGKDAEF EVEDTIKLKG GRVGHLGTVT 550 560 570 580 590 600 KGSFKVGETV TLTIDTQKRQ AIGKNHSATH LLQKALRNVL GSHVEQAGSF VTSERLRFDF 610 620 630 640 650 660 THFSALTKEE IAKVEAMVNE EIAKNVPVVT DVMSVEDAKK SGAMALFGEK YGDSVRVVTM 670 680 690 700 710 720 GDFSKELCGG THVANTGSIT VFKILSEAGI AAGVRRIEAI TSNAVFEYYK SMEEELHEAA 730 740 750 760 770 780 KVAKTEPASL VKRIESLQEE LKTALSENEK LKAKLANNSL GDVMNQVVEV KGVKLLASKV 790 800 810 820 830 840 TDADMNGLRN LGDQLKEKLG ECVILLASAS EDKVNLIAMA TDGAMAKGAH AGNLIKEVAV 850 860 870 LVGGGGGGRP NMAQAGGKNP SGIDAAIEKA VSVVENQIK

References

[1]

"Complete genome sequence of Clostridium phytofermentans ISDg." Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L., LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C. , Han C., Kuske C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.A., Richardson P. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700394 / DSM 18823 / ISDg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000885 Genomic DNA. Translation: ABX42978.1.
RefSeq	YP_001559717.1. NC_010001.1.
3D structure databases
ProteinModelPortal	A9KMW7.
ModBase	Search...
Protein-protein interaction databases
STRING	A9KMW7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5742782.
GenomeReviews	Gene locus Cphy_2617 in contig CP000885_GR.
KEGG	cpy:Cphy_2617.
PATRIC	19504972. VBICloPhy16213_2724.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG354397.
OMA	GESKTDQ.
ProtClustDB	PRK00252.
Enzyme and pathway databases
BioCyc	CPHY357809:CPHY_2617-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.
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

SYA1_CLOPH

Accession

Primary (citable) accession number: A9KMW7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program