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Q9X0C7

- HIS4_THEMA

UniProt

Q9X0C7 - HIS4_THEMA

Protein

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase

Gene

hisA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide = 5-((5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino)-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei8 – 81Proton acceptor1 Publication
    Active sitei127 – 1271Proton donor1 Publication

    GO - Molecular functioni

    1. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. histidine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesis

    Enzyme and pathway databases

    UniPathwayiUPA00031; UER00009.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (EC:5.3.1.16)
    Alternative name(s):
    Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase
    Gene namesi
    Name:hisA
    Ordered Locus Names:TM_1037
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000008183: Chromosome

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi8 – 81D → N: Loss of activity. 1 Publication
    Mutagenesisi48 – 481H → A: Decrease in activity. 1 Publication
    Mutagenesisi51 – 511D → N: Decrease in activity. 1 Publication
    Mutagenesisi83 – 831R → N: Decrease in activity. 1 Publication
    Mutagenesisi127 – 1271D → N: Almost no activity. 1 Publication
    Mutagenesisi164 – 1641T → A: Strong decrease in activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2412411-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerasePRO_0000142068Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi243274.TM1037.

    Structurei

    Secondary structure

    1
    241
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 109
    Beta strandi13 – 175
    Helixi18 – 203
    Helixi22 – 243
    Beta strandi25 – 306
    Helixi32 – 4110
    Beta strandi47 – 515
    Helixi52 – 576
    Helixi63 – 686
    Helixi69 – 757
    Beta strandi76 – 816
    Helixi85 – 939
    Beta strandi98 – 1014
    Helixi103 – 1075
    Helixi111 – 1166
    Turni117 – 1193
    Beta strandi121 – 1299
    Helixi141 – 1444
    Helixi146 – 1549
    Turni155 – 1573
    Beta strandi160 – 1656
    Helixi168 – 1714
    Helixi177 – 18711
    Beta strandi190 – 1967
    Helixi200 – 21213
    Turni213 – 2153
    Beta strandi216 – 2227
    Helixi224 – 2274
    Helixi233 – 2408

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QO2X-ray1.85A/B1-241[»]
    2CFFX-ray2.50A/B1-241[»]
    2W79X-ray1.85A/B1-241[»]
    ProteinModelPortaliQ9X0C7.
    SMRiQ9X0C7. Positions 1-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9X0C7.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the HisA/HisF family.Curated

    Phylogenomic databases

    eggNOGiCOG0106.
    KOiK01814.
    OMAiKKENTIF.
    OrthoDBiEOG6H1Q3W.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01014. HisA.
    InterProiIPR013785. Aldolase_TIM.
    IPR006062. His_biosynth.
    IPR006063. HisA.
    IPR023016. Isoase_HisA.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view]
    PfamiPF00977. His_biosynth. 1 hit.
    [Graphical view]
    SUPFAMiSSF51366. SSF51366. 1 hit.
    TIGRFAMsiTIGR00007. TIGR00007. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9X0C7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLVVPAIDLF RGKVARMIKG RKENTIFYEK DPVELVEKLI EEGFTLIHVV    50
    DLSNAIENSG ENLPVLEKLS EFAEHIQIGG GIRSLDYAEK LRKLGYRRQI 100
    VSSKVLEDPS FLKSLREIDV EPVFSLDTRG GRVAFKGWLA EEEIDPVSLL 150
    KRLKEYGLEE IVHTEIEKDG TLQEHDFSLT KKIAIEAEVK VLAAGGISSE 200
    NSLKTAQKVH TETNGLLKGV IVGRAFLEGI LTVEVMKRYA R 241
    Length:241
    Mass (Da):27,028
    Last modified:November 1, 1999 - v1
    Checksum:iB1ABDDE5A4D5213D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36114.1.
    PIRiD72304.
    RefSeqiNP_228843.1. NC_000853.1.
    YP_007977390.1. NC_021214.1.
    YP_008991867.1. NC_023151.1.

    Genome annotation databases

    EnsemblBacteriaiAAD36114; AAD36114; TM_1037.
    GeneIDi897150.
    KEGGitma:TM1037.
    tmi:THEMA_09175.
    tmm:Tmari_1041.
    PATRICi23937003. VBITheMar51294_1050.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36114.1 .
    PIRi D72304.
    RefSeqi NP_228843.1. NC_000853.1.
    YP_007977390.1. NC_021214.1.
    YP_008991867.1. NC_023151.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QO2 X-ray 1.85 A/B 1-241 [» ]
    2CFF X-ray 2.50 A/B 1-241 [» ]
    2W79 X-ray 1.85 A/B 1-241 [» ]
    ProteinModelPortali Q9X0C7.
    SMRi Q9X0C7. Positions 1-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243274.TM1037.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD36114 ; AAD36114 ; TM_1037 .
    GeneIDi 897150.
    KEGGi tma:TM1037.
    tmi:THEMA_09175.
    tmm:Tmari_1041.
    PATRICi 23937003. VBITheMar51294_1050.

    Phylogenomic databases

    eggNOGi COG0106.
    KOi K01814.
    OMAi KKENTIF.
    OrthoDBi EOG6H1Q3W.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00009 .

    Miscellaneous databases

    EvolutionaryTracei Q9X0C7.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01014. HisA.
    InterProi IPR013785. Aldolase_TIM.
    IPR006062. His_biosynth.
    IPR006063. HisA.
    IPR023016. Isoase_HisA.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view ]
    Pfami PF00977. His_biosynth. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51366. SSF51366. 1 hit.
    TIGRFAMsi TIGR00007. TIGR00007. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    2. "Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substrates."
      Henn-Sax M., Thoma R., Schmidt S., Hennig M., Kirschner K., Sterner R.
      Biochemistry 41:12032-12042(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITES, SUBUNIT, MUTAGENESIS OF ASP-8; HIS-48; ASP-51; ARG-83; ASP-127 AND THR-164.
    3. "Structural evidence for evolution of the beta/alpha barrel scaffold by gene duplication and fusion."
      Lang D., Thoma R., Henn-Sax M., Sterner R., Wilmanns M.
      Science 289:1546-1550(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).

    Entry informationi

    Entry nameiHIS4_THEMA
    AccessioniPrimary (citable) accession number: Q9X0C7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 102 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