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Q65G68 (ARLY_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Argininosuccinate lyase

Short name=ASAL
EC=4.3.2.1
Alternative name(s):
Arginosuccinase
Gene names
Name:argH
Ordered Locus Names:BLi03083, BL00416
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Protein existenceInferred 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 By similarity HAMAP MF_00006.

Sequence similarities

Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine biosynthetic process via ornithine

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionargininosuccinate lyase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Argininosuccinate lyase HAMAP MF_00006
PRO_0000240714

Sequences

Sequence LengthMass (Da)Tools
Q65G68 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 7EE1D6F5B2682D89

FASTA45951,981
        10         20         30         40         50         60 
MKKLWGGRFQ KTPEKWVDEF GASIHFDKTL VKEDIAGSLA HASMLEKCGI LTEAEAVKIK 

        70         80         90        100        110        120 
EGLTSLLHKA EKNELDFSVD CEDIHLNLEK MLIDEIGPLG GKLHTARSRN DQVATDMHLY 

       130        140        150        160        170        180 
LKGHTEHIIE LITAFQHVLI EKAEEHVETI LPGYTHLQRA QPISFAHHLL AYFWMLERDK 

       190        200        210        220        230        240 
ERYHDSFKRI NKSPLGCGAL AGTTFPIDRE YSADLLGFDS IYENSLDGVS DRDFILEFLS 

       250        260        270        280        290        300 
ASSILMMHLS RFSEEIILWC SQEFKFIELD DTYATGSSMM PQKKNPDMAE LIRGKTGRVY 

       310        320        330        340        350        360 
GDLIGLLTIM KGLPLAYNKD LQEDKEGMFD TVKTVEGSLE IFAGMIKTMT VNKNMMKKAT 

       370        380        390        400        410        420 
EQDFSNATEL ADYLAKKGMP FREAHEVVGR LVFTCIEKGI YLSGLPFEEF KKASGLFEED 

       430        440        450 
VYIVLDPHHA VEKRMSEGGT GFKKVTEAIQ KAKQCLNNF 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017333 Genomic DNA. Translation: AAU41946.1.
CP000002 Genomic DNA. Translation: AAU24588.1.
RefSeqYP_080226.1. NC_006270.3.
YP_092639.1. NC_006322.1.

3D structure databases

ProteinModelPortalQ65G68.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ65G68.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000054359; EBBACP00000052890; EBBACG00000054350.
EBBACT00000058854; EBBACP00000057287; EBBACG00000058845.
GeneID3028973.
3098707.
GenomeReviewsGene locus BLi03083 in contig AE017333_GR.
Gene locus BL00416 in contig CP000002_GR.
KEGGbld:BLi03083.
bli:BL00416.
NMPDRfig|279010.5.peg.3444.
PATRIC18951902. VBIBacLic203714_3151.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0165.
GeneTreeEBGT00070000031828.
HOGENOMHBG539632.
OMAMAEDLIF.
PhylomeDBQ65G68.
ProtClustDBPRK00855.

Enzyme and pathway databases

BioCycBLIC279010-1:BLI03083-MONOMER.
BLIC279010:BL00416-MONOMER.

Family and domain databases

HAMAPMF_00006. Arg_succ_lyase.
[Tree]
InterProIPR009049. Argininosuccinate_lyase.
IPR003031. D_crystallin.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR008948. L-Aspartase-like.
IPR022761. Lyase1_N.
[Graphical view]
KOK01755.
PANTHERPTHR11444:SF3. argH. 1 hit.
PfamPF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00145. ARGSUCLYASE.
PR00149. FUMRATELYASE.
SUPFAMSSF48557. L-Aspartase-like. 1 hit.
TIGRFAMsTIGR00838. ArgH. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARLY_BACLD
AccessionPrimary (citable) accession number: Q65G68
Secondary accession number(s): Q62RM2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families