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P59846

- ASSY_THET8

UniProt

P59846 - ASSY_THET8

Protein

Argininosuccinate synthase

Gene

argG

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (19 Sep 2003)
      Previous versions | rss
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    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 oxygen2 PublicationsUniRule annotation
    Binding sitei84 – 841Citrulline
    Binding sitei89 – 891Citrulline
    Binding sitei114 – 1141ATP; via amide nitrogen2 PublicationsUniRule annotation
    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 – 149ATP2 PublicationsUniRule 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

    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 synthaseUniRule annotation (EC:6.3.4.5UniRule annotation)
    Alternative name(s):
    Citrulline--aspartate ligaseUniRule annotation
    Gene namesi
    Name:argGUniRule annotation
    Ordered Locus Names:TTHA0284
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000532: Chromosome

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 400400Argininosuccinate synthasePRO_0000148658Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.2 PublicationsUniRule annotation

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP59846.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the argininosuccinate synthase family. Type 1 subfamily.UniRule annotation

    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.

    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

    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: October 1, 2014
    This is version 86 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