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P59846

- ASSY_THET8

UniProt

P59846 - ASSY_THET8

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Protein

Argininosuccinate synthase

Gene
argG, TTHA0284
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331ATP; via amide nitrogen and carbonyl oxygen
Binding sitei84 – 841Citrulline
Binding sitei89 – 891Citrulline
Binding sitei114 – 1141ATP; via amide nitrogen
Binding sitei116 – 1161Aspartate
Binding sitei120 – 1201Aspartate
Binding sitei120 – 1201Citrulline
Binding sitei121 – 1211Aspartate
Binding sitei124 – 1241Citrulline
Binding sitei173 – 1731Citrulline
Binding sitei182 – 1821Citrulline
Binding sitei258 – 2581Citrulline
Binding sitei270 – 2701Citrulline

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi6 – 149ATPUniRule annotation

GO - Molecular functioni

  1. argininosuccinate synthase activity Source: UniProtKB-HAMAP
  2. ATP binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. arginine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-298-MONOMER.
UniPathwayiUPA00068; UER00113.

Names & Taxonomyi

Protein namesi
Recommended name:
Argininosuccinate synthase (EC:6.3.4.5)
Alternative name(s):
Citrulline--aspartate ligase
Gene namesi
Name:argG
Ordered Locus Names:TTHA0284
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

Subcellular locationi

Cytoplasm Inferred UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 400400Argininosuccinate synthaseUniRule annotationPRO_0000148658Add
BLAST

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

STRINGi300852.TTHA0284.

Structurei

Secondary structure

1
400
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Helixi11 – 2414
Beta strandi27 – 3610
Helixi41 – 5111
Beta strandi54 – 607
Helixi62 – 687
Helixi70 – 756
Turni81 – 833
Turni87 – 904
Helixi91 – 10616
Beta strandi109 – 1124
Beta strandi117 – 1204
Helixi121 – 13212
Beta strandi137 – 1393
Helixi141 – 1433
Helixi150 – 15910
Beta strandi173 – 1764
Beta strandi181 – 1855
Helixi186 – 1894
Beta strandi201 – 2033
Helixi206 – 2083
Beta strandi214 – 2218
Beta strandi224 – 2285
Helixi235 – 24814
Beta strandi253 – 2597
Beta strandi265 – 2717
Helixi273 – 28917
Helixi292 – 31120
Beta strandi314 – 3163
Helixi317 – 33014
Beta strandi335 – 3428
Beta strandi345 – 3528
Helixi360 – 3623
Helixi373 – 39422

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J1ZX-ray2.10A/B/C/D1-400[»]
1J20X-ray2.00A/B/C/D1-400[»]
1J21X-ray2.20A/B/C/D1-400[»]
1KH1X-ray2.30A/B/C/D1-400[»]
1KH2X-ray2.30A/B/C/D1-400[»]
1KH3X-ray2.15A/B/C/D1-400[»]
1KORX-ray1.95A/B/C/D1-400[»]
ProteinModelPortaliP59846.
SMRiP59846. Positions 1-395.

Miscellaneous databases

EvolutionaryTraceiP59846.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0137.
HOGENOMiHOG000230093.
KOiK01940.
OMAiAPPEEAY.
OrthoDBiEOG6K9QCV.
PhylomeDBiP59846.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00005. Arg_succ_synth_type1.
InterProiIPR001518. 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]
PfamiPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00032. argG. 1 hit.
PROSITEiPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P59846-1 [UniParc]FASTAAdd to Basket

« Hide

MKIVLAYSGG LDTSIILKWL KETYRAEVIA FTADIGQGEE VEEAREKALR    50
TGASKAIALD LKEEFVRDFV FPMMRAGAVY EGYYLLGTSI ARPLIAKHLV 100
RIAEEEGAEA IAHGATGKGN DQVRFELTAY ALKPDIKVIA PWREWSFQGR 150
KEMIAYAEAH GIPVPVTQEK PYSMDANLLH ISYEGGVLED PWAEPPKGMF 200
RMTQDPEEAP DAPEYVEVEF FEGDPVAVNG ERLSPAALLQ RLNEIGGRHG 250
VGRVDIVENR FVGMKSRGVY ETPGGTILYH ARRAVESLTL DREVLHQRDM 300
LSPKYAELVY YGFWYAPERE ALQAYFDHVA RSVTGVARLK LYKGNVYVVG 350
RKAPKSLYRQ DLVSFDEAGG YDQKDAEGFI KIQALRLRVR ALVEREGHGA 400
Length:400
Mass (Da):44,816
Last modified:September 19, 2003 - v1
Checksum:iA4DAC90A7C5185C6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008226 Genomic DNA. Translation: BAD70107.1.
RefSeqiYP_143550.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70107; BAD70107; BAD70107.
GeneIDi3168176.
KEGGittj:TTHA0284.
PATRICi23955523. VBITheThe93045_0284.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008226 Genomic DNA. Translation: BAD70107.1 .
RefSeqi YP_143550.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J1Z X-ray 2.10 A/B/C/D 1-400 [» ]
1J20 X-ray 2.00 A/B/C/D 1-400 [» ]
1J21 X-ray 2.20 A/B/C/D 1-400 [» ]
1KH1 X-ray 2.30 A/B/C/D 1-400 [» ]
1KH2 X-ray 2.30 A/B/C/D 1-400 [» ]
1KH3 X-ray 2.15 A/B/C/D 1-400 [» ]
1KOR X-ray 1.95 A/B/C/D 1-400 [» ]
ProteinModelPortali P59846.
SMRi P59846. Positions 1-395.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300852.TTHA0284.

Chemistry

DrugBanki DB00131. Adenosine monophosphate.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD70107 ; BAD70107 ; BAD70107 .
GeneIDi 3168176.
KEGGi ttj:TTHA0284.
PATRICi 23955523. VBITheThe93045_0284.

Phylogenomic databases

eggNOGi COG0137.
HOGENOMi HOG000230093.
KOi K01940.
OMAi APPEEAY.
OrthoDBi EOG6K9QCV.
PhylomeDBi P59846.

Enzyme and pathway databases

UniPathwayi UPA00068 ; UER00113 .
BioCyci TTHE300852:GH8R-298-MONOMER.

Miscellaneous databases

EvolutionaryTracei P59846.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPi MF_00005. Arg_succ_synth_type1.
InterProi IPR001518. 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 ]
Pfami PF00764. Arginosuc_synth. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00032. argG. 1 hit.
PROSITEi PS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  2. "Crystal structure of argininosuccinate synthetase from Thermus thermophilus HB8. Structural basis for the catalytic action."
    Goto M., Nakajima Y., Hirotsu K.
    J. Biol. Chem. 277:15890-15896(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ATP AND SUBSTRATE ANALOGS, SUBUNIT.
  3. "Structures of argininosuccinate synthetase in enzyme-ATP substrates and enzyme-AMP product forms: stereochemistry of the catalytic reaction."
    Goto M., Omi R., Miyahara I., Sugahara M., Hirotsu K.
    J. Biol. Chem. 278:22964-22971(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP AND SUBSTRATES, SUBUNIT.

Entry informationi

Entry nameiASSY_THET8
AccessioniPrimary (citable) accession number: P59846
Secondary accession number(s): Q5SLK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: September 19, 2003
Last modified: July 9, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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