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A4J174 (ARLY_DESRM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Dred_0278
OrganismDesulfotomaculum reducens (strain MI-1) [Complete proteome] [HAMAP]
Taxonomic identifier349161 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Peptococcaceae › Desulfotomaculum ›

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

2-(N(omega)-L-arginino)succinate = fumarate + L-arginine. HAMAP-Rule MF_00006

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. HAMAP-Rule MF_00006

Subcellular location

Cytoplasm By similarity.

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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 460460Argininosuccinate lyase HAMAP-Rule MF_00006
PRO_1000070920

Sequences

Sequence LengthMass (Da)Tools
A4J174 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: C80036007A562731

FASTA46051,274
        10         20         30         40         50         60 
MKLWGGRFQK TTDSLVEDFH SSISFDQRLY KQDIRGSIAH ATMLGKVGII SLEEAAQIVT 

        70         80         90        100        110        120 
GLKQILEEIE AGKVEFDVAA EDIHMNVEQL LTAKIGAVGK KLHTARSRND QVAVDIRMYL 

       130        140        150        160        170        180 
KDEIIEIRAL LKELVETLLN LAEQHTNTVM PGYTHMQRAQ PITFAHHLMA YSQMFMRDMG 

       190        200        210        220        230        240 
RLTDCYKRTD VMPLGSGALA GTTFPLDREY TAELLGFAAV SDNSLDAVSD RDFAVEFCAA 

       250        260        270        280        290        300 
ASLIMMHLSR FCEEIILWAT GEFAFIDLDD AYSTGSSIMP QKKNPDVAEL IRGKTGRVYG 

       310        320        330        340        350        360 
DLMGLLTMLK GLPMAYNKDM QEDKEALFDA MDTVKGCLMV FRPMLATMTV RQENMAKAAR 

       370        380        390        400        410        420 
GGFTNATDVA DYLAKKGVPF REAHEVVGKA VFYCLQQNKA LEELTLEEYK ELSPVFEDDI 

       430        440        450        460 
YAAIGVEYCV AARKVRGGPA PEAVQQAITR TKERLKQLGE

« Hide

References

[1]"Complete sequence of Desulfotomaculum reducens MI-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MI-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000612 Genomic DNA. Translation: ABO48827.1.
RefSeqYP_001111652.1. NC_009253.1.

3D structure databases

ProteinModelPortalA4J174.
ModBaseSearch...

Protein-protein interaction databases

STRING349161.Dred_0278.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO48827; ABO48827; Dred_0278.
GeneID4957177.
KEGGdrm:Dred_0278.
PATRIC21726358. VBIDesRed82656_0288.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0165.
HOGENOMHOG000242744.
KOK01755.
OMAEDIHTVI.
ProtClustDBPRK00855.

Enzyme and pathway databases

BioCycDRED349161:GHP6-378-MONOMER.
UniPathwayUPA00068; UER00114.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
HAMAPMF_00006. Arg_succ_lyase.
InterProIPR009049. Argininosuccinate_lyase.
IPR003031. D_crystallin.
IPR024083. Fumarase/histidase_N.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERPTHR11444:SF3. PTHR11444:SF3. 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_DESRM
AccessionPrimary (citable) accession number: A4J174
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 1, 2007
Last modified: May 1, 2013
This is version 46 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

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