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B0CEZ5 (ARLY_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 32. 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:AM1_4415
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Chroococcales › Acaryochloris

Protein attributes

Sequence length476 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 – 476476Argininosuccinate lyase HAMAP MF_00006
PRO_0000335822

Sequences

Sequence LengthMass (Da)Tools
B0CEZ5 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 42093BB483AD1EC1

FASTA47652,917
        10         20         30         40         50         60 
MTSSPVPPTN SSDSSDSKVW SQRFESALNP VIAAFNASIH FDIALIEYDL TGSQAHVQML 

        70         80         90        100        110        120 
AHSGIISQAE ADAIDQGLEA IRQEYRQGQF QPGIEAEDIH FAVENRLIEL IGDTGKKLHT 

       130        140        150        160        170        180 
GRSRNDQVGT DLRLYLHDQI LQVQTLIRNW QQALVILASD HVQTLIPGYT HLQRAQPISL 

       190        200        210        220        230        240 
AHHLLAYFEM AERDWQRLRE IDRRVNVSPL GLGALAGTPF PIDRQYTADK LGFADLYRNS 

       250        260        270        280        290        300 
LDGVSDRDFA IEFLCAASLI MVHLSRFSEE VILWASEEFG FIKLKDSCAT GSSIMPQKKN 

       310        320        330        340        350        360 
PDVPELVRGK SGRVFGHLQS LLVVMKGLPL AYNKDLQEDK EAIFDGVTTI KACLEAMTIL 

       370        380        390        400        410        420 
VAEGLEFQTP RLESAVGEDF SNATDVADYL SKQGVPFREA YNIVGAVVKT CLSQNKLLKD 

       430        440        450        460        470 
LTLEEWQQFH PQFADDIYSA ISPRQVVAVR NSFGGTGFTQ VQNALEQAKT LLSQSK

« Hide

References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBIC 11017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000828 Genomic DNA. Translation: ABW29392.1.
RefSeqYP_001518709.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0CEZ5.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0CEZ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5683217.
GenomeReviewsGene locus AM1_4415 in contig CP000828_GR.
KEGGamr:AM1_4415.
PATRIC20622916. VBIAcaMar40141_4079.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG539632.
OMAMAEDLIF.
PhylomeDBB0CEZ5.
ProtClustDBPRK00855.

Enzyme and pathway databases

BioCycAMAR329726:AM1_4415-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_ACAM1
AccessionPrimary (citable) accession number: B0CEZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 32 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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