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A0M369 (A0M369_GRAFK) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Argininosuccinate lyase HAMAP MF_00006

Short name=ASAL HAMAP MF_00006
EC=4.3.2.1 HAMAP MF_00006
Alternative name(s):
Arginosuccinase HAMAP MF_00006
Gene names
Name:argH HAMAP MF_00006 EMBL CAL67064.1
Ordered Locus Names:GFO_2099
OrganismGramella forsetii (strain KT0803) [Complete proteome] [HAMAP]
Taxonomic identifier411154 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeGramella

Protein attributes

Sequence length429 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. HAMAP MF_00006

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis HAMAP MF_00006
   Cellular componentCytoplasm HAMAP MF_00006
   Molecular functionLyase HAMAP MF_00006 EMBL CAL67064.1
   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...

Sequences

Sequence LengthMass (Da)Tools
A0M369 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: B6D270BB3E5B69D4

FASTA42948,771
        10         20         30         40         50         60 
MKLWDKGISI DKQIEKFTVG NDRELDMHLA EYDIQASKAH AKMLGKVGIL EKDEVETILT 

        70         80         90        100        110        120 
ELEVLKKQLE NGLFHIEEDF EDVHSKIEFE LTKKLGDTGK KIHTARSRND QVLVAQQLYF 

       130        140        150        160        170        180 
KENLQQISEK AKELIEVLLG LADEHKEKLL PGYTHLQVAM PSSFGLWFSA YAELLIDDLY 

       190        200        210        220        230        240 
LLEAGLKIVD QNPLGSAAGY GSSFPIDREF TTRELGFSTQ KFNVVAAQMS RGKCERTVTS 

       250        260        270        280        290        300 
NIASLANTLS RLAMDICLYM SQNFDFITFP DELTTGSSIM PHKKNPDVFE LVRGKCNKLQ 

       310        320        330        340        350        360 
AIANEMILIT NNLPSGYHRD FQLIKENSIY SVENMKEILD VFTHSIAQIK VKNVDLKDEK 

       370        380        390        400        410        420 
YKYLFTVDSI NELVINGKSF RDAYKIIGEQ VQDGSYKATE GMQHSHSGSK DNLSLEKIRE 


KKEEINLKI 

« Hide

References

[1]"Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter."
Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O.
Environ. Microbiol. 8:2201-2213(2006) [PubMed: 17107561] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU207366 Genomic DNA. Translation: CAL67064.1.
RefSeqYP_862131.1. NC_008571.1.

3D structure databases

ProteinModelPortalA0M369.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0M369.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4652594.
GenomeReviewsGene locus GFO_2099 in contig CU207366_GR.
KEGGgfo:GFO_2099.
NMPDRfig|411154.5.peg.1988.
PATRIC22072973. VBIGraFor5527_2024.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0165.
HOGENOMHBG539632.
OMAKKNPDVF.
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 nameA0M369_GRAFK
AccessionPrimary (citable) accession number: A0M369
Entry history
Integrated into UniProtKB/TrEMBL: December 12, 2006
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)