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Q123L8 (Q123L8_POLSJ) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 41. 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 2 HAMAP MF_00006
Short name=ASAL 2 HAMAP MF_00006
EC=4.3.2.1 HAMAP MF_00006
Alternative name(s):
Arginosuccinase 2 HAMAP MF_00006
Gene names
Name:argH2 HAMAP MF_00006
Ordered Locus Names:Bpro_4386
OrganismPolaromonas sp. (strain JS666 / ATCC BAA-500) [Complete proteome] [HAMAP]
Taxonomic identifier296591 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Polaromonas

Protein attributes

Sequence length499 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 ABE46274.1
   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
Q123L8 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: FF3C3C9BD7198027

FASTA49954,664
        10         20         30         40         50         60 
MESKVSRRLK EPTAKEICEH ITGPRLARDF PRQFPYLTVV NQAHLLMLHK TGLISPDVAK 

        70         80         90        100        110        120 
KLANGLAQME AEGPEAVELD PAKEEPYFNY ESKLMEIVGR DVGGRLHMAR SRNDIGVTID 

       130        140        150        160        170        180 
RLRARSAVLN VLEALGRVRR VALERASKFT NVIMPGYTHL QPAQPITYGF YLSAVAEALG 

       190        200        210        220        230        240 
RDMDRLHASL ARIDESPLGA GALAGTRFPI DRSVTATALG FSSVAPNTLD AVASRDFAWE 

       250        260        270        280        290        300 
AMSAMTIVAL TWGRVAQDFQ VWSTLEFGLV SFPDRVASTS SIMPQKKNPV VLEYLRGKSS 

       310        320        330        340        350        360 
HIIGLLTASL VAVKGTHFTH AGDSSRESMR SFWECAEETL RCLALFELIV STAEPKEKNM 

       370        380        390        400        410        420 
LQHVRFDFSV ATDLADGLVA EAGMSFREAH HVVGGLVRLA LDEGKSANEL TSAMLDRAAV 

       430        440        450        460        470        480 
DVIGSAIEWP EQKLRKYLDP IECVNMRHNG GPAPAELSGA IKKQLGSLEN VLAKVQSTRD 

       490 
HFTAAHEQMK RDVAAIASQ

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References

[1]"Complete sequence of chromosome of Polaromonas sp. JS666."
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., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JS666 / ATCC BAA-500.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000316 Genomic DNA. Translation: ABE46274.1.
RefSeqYP_551172.1. NC_007948.1.

3D structure databases

ProteinModelPortalQ123L8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ123L8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4012957.
GenomeReviewsGene locus Bpro_4386 in contig CP000316_GR.
KEGGpol:Bpro_4386.
NMPDRfig|296591.1.peg.989.
PATRIC22962038. VBIPolSp102244_4466.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0165.
HOGENOMHBG539632.
OMAGMEREHE.
ProtClustDBCLSK953291.

Enzyme and pathway databases

BioCycPSP296591:BPRO_4386-MONOMER.

Family and domain databases

HAMAPMF_00006. Arg_succ_lyase.
[Tree]
InterProIPR009049. Argininosuccinate_lyase.
IPR003031. D_crystallin.
IPR000362. Fumarate_lyase.
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.
ProtoNetSearch...

Entry information

Entry nameQ123L8_POLSJ
AccessionPrimary (citable) accession number: Q123L8
Entry history
Integrated into UniProtKB/TrEMBL: August 22, 2006
Last sequence update: August 22, 2006
Last modified: December 14, 2011
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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