Reviewed, UniProtKB/Swiss-Prot Q8KA59 (ARLY_BUCAP)

Names and origin

Protein names

Recommended name:
    Argininosuccinate lyase
      Short name(s)=ASAL, Arginosuccinase
    EC=4.3.2.1

Gene names

Name:	argH
Ordered Locus Names:	BUsg_048

Organism

Buchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]

Taxonomic identifier

98794 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	459 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	2-(N(omega)-L-arginino)succinate = fumarate + L-arginine.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.
Subcellular location	CytoplasmProbable.
Sequence similarities	Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
Molecular function	argininosuccinate lyase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 459	459	Argininosuccinate lyase

Sequences

	Sequence		Length	Mass (Da)
	Q8KA59-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: ADD7D45577219C6A	FASTA	459	52,044
	10 20 30 40 50 60 MSLWGGRFLD ESNETFKKFN ASLPFDYILV KEDIFASIAW SKSLVEVGVL TQEEQKKIES 70 80 90 100 110 120 ALISLKEEIY NNSKKILESD YEDIHSWIEA NLIKKIGELG KKLHTGRSRN DQITTDLKLW 130 140 150 160 170 180 CKRKIFVLLD SIINLQKNFI FVAELNDDVI MPGYTHLQRA QPITFSYWCL AYVQMFKRDV 190 200 210 220 230 240 SRLKDILKRL DISPLGSGAL SGTAWNINRK KLAISMGFSS ETNNALDSVS DRDYLIELLS 250 260 270 280 290 300 ASSISMTHLS RFSEDLIFFN SSEANFIELS DSITSGSSLM PQKKNPDALE LIRAKCGRVH 310 320 330 340 350 360 GALVSILVVL KSLPLSYNKD LQEDKEGLFD SLKTWNDSLL IASLVLKNIK LNRLSCRKAA 370 380 390 400 410 420 EKGYSNATEI ADYLVKKGMT FREAHHVSGK LVLRAIKENK SLNDLDLSIF QSYSALITDD 430 440 450 IYKNITLEAC LEKRSSKGGV APNEIRKEIF KEKERLNIL

References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE013218 Genomic DNA. Translation: AAM67619.1.
RefSeq	NP_660408.1.
3D structure databases
HSSP	HSSP built from PDB template 1AOS based on UniProtKB P04424.
ModBase	Search...
Genome annotation databases
GeneID	1005864.
GenomeReviews	Gene locus BUsg_048 in contig AE013218_GR.
KEGG	bas:BUsg048.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8KA59.
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG048-MON.
Family and domain databases
HAMAP	MF_00006. [Tree]
InterPro	IPR009049. Argininosuccinate_lyase. IPR003031. D_crystallin. IPR000362. Fumarate_lyase. [Graphical view]
PANTHER	PTHR11444:SF3. argH. 1 hit.
Pfam	PF00206. Lyase_1. 1 hit. [Graphical view]
PRINTS	PR00145. DCRYSTALLIN. PR00149. FUMRATELYASE.
TIGRFAMs	TIGR00838. argH. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProDom	Q8KA59. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

ARLY_BUCAP

Accession

Primary (citable) accession number: Q8KA59

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	October 1, 2002
Last modified:	July 22, 2008
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)