Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q64Z15 (ARLY_BACFR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. 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:BF0512
OrganismBacteroides fragilis (strain YCH46) [Complete proteome] [HAMAP]
Taxonomic identifier295405 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length447 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 – 447447Argininosuccinate lyase HAMAP MF_00006
PRO_1000116308

Sequences

Sequence LengthMass (Da)Tools
Q64Z15 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 5634462A32C875DC

FASTA44750,813
        10         20         30         40         50         60 
MAQKLWEKSV EVNKDIERFT VGRDREMDLY LAKHDVLGSM AHITMLESIG LLTKEELAQL 

        70         80         90        100        110        120 
LTELKDIYAS AERGEFVIEE GVEDVHSQVE LMLTRRLGDV GKKIHSGRSR NDQVLLDLKL 

       130        140        150        160        170        180 
FTRTQIREVA EAVEQLFHVL IRQSERYKNV LMPGYTHLQI AMPSSFGLWF GAYAESLVDD 

       190        200        210        220        230        240 
MLFLQAAFKM CNKNPLGSAA GYGSSFPLNR TMTTELLGFD SLNYNVVYAQ MGRGKMERNV 

       250        260        270        280        290        300 
AFALATLAGT ISKLAFDACM FNSQNFGFVK LPDECTTGSS IMPHKKNPDV FELTRAKCNK 

       310        320        330        340        350        360 
LQSLPQQIMM IANNLPSGYF RDLQIIKEVF LPAFQELKDC LQMTTYIMNE IKVNEHILDD 

       370        380        390        400        410        420 
DKYLFIFSVE EVNRLAREGM PFRDAYKKVG LDIEAGHFSH DKQVHHTHEG SIGNLCNDEI 

       430        440 
SALMQRTIEG FNFQGMEQAE KTLLGRK 

« Hide

References

[1]"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed: 15466707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YCH46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006841 Genomic DNA. Translation: BAD47261.1.
RefSeqYP_097795.1. NC_006347.1.

3D structure databases

HSSPHSSP built from PDB template 1AOS based on UniProtKB P04424.
ProteinModelPortalQ64Z15.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3082258.
GenomeReviewsGene locus BF0512 in contig AP006841_GR.
KEGGbfr:BF0512.
NMPDRfig|295405.3.peg.334.
PATRIC21046790. VBIBacFra17906_0528.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG539632.
OMAKKNPDVF.
ProtClustDBPRK00855.

Enzyme and pathway databases

BioCycBFRA295405:BF0512-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_BACFR
AccessionPrimary (citable) accession number: Q64Z15
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 57 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