Reviewed, UniProtKB/Swiss-Prot A3MLL6 (ARLY_BURM7)

Names and origin

Protein names

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

Gene names

Name:	argH
Ordered Locus Names:	BMA10247_1608

Organism

Burkholderia mallei (strain NCTC 10247) [Complete proteome] [HAMAP]

Taxonomic identifier

320389 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	469 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	2-(N(omega)-L-arginino)succinate = fumarate + L-arginine. HAMAP MF_00006
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. HAMAP MF_00006
Subcellular location	Cytoplasm Probable HAMAP MF_00006.
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)
Biological process	arginine biosynthetic process via ornithine Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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	Feature identifier
Molecule processing
	Chain	1 – 469	469	Argininosuccinate lyase HAMAP MF_00006		PRO_1000000458

Sequences

	Sequence		Length	Mass (Da)
	A3MLL6-1 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: 9DEA731475F7D25B	FASTA	469	51,173
	10 20 30 40 50 60 MTSQLHKKGE AWSARFSEPM SELVKRYTSS VFFDKRLALV DIAGSLAHAG MLAAQKIISA 70 80 90 100 110 120 DDLAAIERGM AQIKGEIERG EFEWQLDLED VHLNIEARLT ALIGDAGKRL HTGRSRNDQV 130 140 150 160 170 180 ATDIRLWLRG EIDRIGGLLN DLRGALIDLA EQNADTILPG FTHLQVAQPV TFGHHLLAYV 190 200 210 220 230 240 EMFSRDAERM RDCRARVNRL PLGAAALAGT SYPIDRHAVA KTLGFDGICA NSLDAVSDRD 250 260 270 280 290 300 FAIEFTAAAA LVMTHVSRFS EELVLWMSPR VGFIDIADRF CTGSSIMPQK KNPDVPELAR 310 320 330 340 350 360 GKTGRVNGHL MALLTLMKGQ PLAYNKDNQE DKEPLFDTVD TVADTLRIFA EMVAGITVKP 370 380 390 400 410 420 DAMRAAALQG FSTATDLADY LVKRGLPFRD AHEAVAHAVK VCDARGIDLA DLTLDEMKQE 430 440 450 460 LPNVAHLIGE DVFDYLTLEG SVASRNHPGG TAPDQVRAAA KAARAALGQ

References

[1]	DeShazer D., Woods D.E., Nierman W.C. Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000548 Genomic DNA. Translation: ABO07282.1.
RefSeq	YP_001081152.1.
3D structure databases
SMR	A3MLL6. Positions 21-468.
ModBase	Search...
Genome annotation databases
GeneID	4893124.
GenomeReviews	Gene locus BMA10247_1608 in contig CP000548_GR.
KEGG	bmn:BMA10247_1608.
TIGR	BMA10247_1608.
Phylogenomic databases
HOGENOM	HBG539632.
OMA	MAEDLIF.
Family and domain databases
HAMAP	MF_00006. Arg_succ_lyase. [Tree]
InterPro	IPR009049. Argininosuccinate_lyase. IPR003031. D_crystallin. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR008948. L-Aspartase-like. [Graphical view]
PANTHER	PTHR11444:SF3. argH. 1 hit.
Pfam	PF00206. Lyase_1. 1 hit. [Graphical view]
PRINTS	PR00145. ARGSUCLYASE. PR00149. FUMRATELYASE.
TIGRFAMs	TIGR00838. argH. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARLY_BURM7

Accession

Primary (citable) accession number: A3MLL6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	April 3, 2007
Last modified:	February 9, 2010
This is version 25 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)