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Q9HKF1 (ASSY_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. 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 synthase

EC=6.3.4.5
Alternative name(s):
Citrulline--aspartate ligase
Gene names
Name:argG
Ordered Locus Names:Ta0650
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length402 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. HAMAP-Rule MF_00005

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP-Rule MF_00005

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00005

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00005.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 1 subfamily.

Sequence caution

The sequence CAC11788.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

argininosuccinate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 402402Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148688

Regions

Nucleotide binding7 – 159ATP By similarity

Sites

Binding site831Citrulline By similarity
Binding site1131ATP; via amide nitrogen By similarity
Binding site1151Aspartate By similarity
Binding site1191Aspartate By similarity
Binding site1191Citrulline By similarity
Binding site1201Aspartate By similarity
Binding site1231Citrulline By similarity
Binding site1691Citrulline By similarity
Binding site1781Citrulline By similarity
Binding site2531Citrulline By similarity
Binding site2651Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HKF1 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: C0A76320E885B537

FASTA40244,813
        10         20         30         40         50         60 
MDKALLLYSG GLDTSVMIKW IQENLSMDVA TLTLNVGNSD LVAIEEKARM LGADPVFVHD 

        70         80         90        100        110        120 
AKDEFAEKFI AKSIMANGSY EGYPLSTALA RPLMAEKAVK YAQKIGAKYI VHGSTGRGND 

       130        140        150        160        170        180 
QVRFEVSIRA LDPSMQVLVP VREWNMMRKD EVEYAKTHGI PVKLDGKYSI DENIWGRSVE 

       190        200        210        220        230        240 
GPDLEDIGKG VPEDVYEWVV PPWKANAEHT LKIAFDGGIP SEIDGEKMKL ADLIVFLNTL 

       250        260        270        280        290        300 
AGSSGIGLID HMENRVVGLK SHEVYECPAA TVITHAHRYL ESLILNRNEA EVKMNMDWQF 

       310        320        330        340        350        360 
AKFVYGGLWH DPVMNAVNAA EAEFNRDISG EIKIRMSHGI MYIEGAWGNS FLYSKDLINY 

       370        380        390        400 
SSMAFDQRAS KGFIDIYGNA TVHSHNRNPK MVKEVQGSSV EF 

« Hide

References

[1]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL445065 Genomic DNA. Translation: CAC11788.1. Different initiation.
RefSeqNP_394121.1. NC_002578.1.

3D structure databases

ProteinModelPortalQ9HKF1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273075.Ta0650.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC11788; CAC11788; CAC11788.
GeneID1456223.
KEGGtac:Ta0650.

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAIYNGYWW.
ProtClustDBPRK00509.

Enzyme and pathway databases

UniPathwayUPA00068; UER00113.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPMF_00005. Arg_succ_synth_type1.
InterProIPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR023434. Arginosuc_synth_type_1_subfam.
IPR024074. AS_cat/multimer_dom_body.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsTIGR00032. argG. 1 hit.
PROSITEPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASSY_THEAC
AccessionPrimary (citable) accession number: Q9HKF1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: December 12, 2006
Last modified: February 19, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways