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A7H771 (ARLY_ANADF) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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:Anae109_0352
OrganismAnaeromyxobacter sp. (strain Fw109-5) [Complete proteome] [HAMAP]
Taxonomic identifier404589 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length474 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 – 474474Argininosuccinate lyase HAMAP MF_00006
PRO_0000321427

Sequences

Sequence LengthMass (Da)Tools
A7H771 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 1DFB764B8E632C12

FASTA47450,914
        10         20         30         40         50         60 
MLASPPPMSA KTKSKPVSRA ALAGEADPRL VALSVSIQDD GALYAEDIRG SQAHVTMLAE 

        70         80         90        100        110        120 
QGIVPKASAR RIVAALDQVR AEFAAGKIRL DPALEDVHTH VERRLGELVG ADAGYLHAGR 

       130        140        150        160        170        180 
SRNDQVALDE RLFIVAACER CDAALGRLQR ALVARAREHE KTILPGYTHL QRAQPVSLAH 

       190        200        210        220        230        240 
HLLAHVEAFA RDRDRLADVR RRAAVSPLGS GALAGTTLPL DREATAKALG LAGVTQNSLD 

       250        260        270        280        290        300 
AVSDRDSAIE LLFACALAAV HLSRVGEEIV LWTTKEFGFM TLADAFATGS SLMPQKKNPD 

       310        320        330        340        350        360 
VGELARGRAG RAIGDLVALL AIVKSLPLSY NRDMQEDKRP LIGGPDALVL TADAVGGAIE 

       370        380        390        400        410        420 
TATFHADRME EALGSGEALA TDAAEYLVER GVPFREAHEA VGKAAAFSSA EGRPLAKLTA 

       430        440        450        460        470 
DEWRRFHPAF QKDVLRCFDA RKSLARRELT GAPGPRQVAR QLARWEKALA KERR 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter sp. Fw109-5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Lykidis A., Fields M., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Fw109-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000769 Genomic DNA. Translation: ABS24567.1.
RefSeqYP_001377551.1. NC_009675.1.

3D structure databases

ProteinModelPortalA7H771.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7H771.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5374894.
GenomeReviewsGene locus Anae109_0352 in contig CP000769_GR.
KEGGafw:Anae109_0352.
NMPDRfig|404589.4.peg.319.
PATRIC20925767. VBIAnaSp113478_0372.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0165.
HOGENOMHBG539632.
OMAMAEDLIF.
ProtClustDBPRK00855.

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_ANADF
AccessionPrimary (citable) accession number: A7H771
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: September 11, 2007
Last modified: January 25, 2012
This is version 36 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