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O74712

- HIS2_CANAX

UniProt

O74712 - HIS2_CANAX

Protein

Histidine biosynthesis trifunctional protein

Gene

HIS4

Organism
Candida albicans (Yeast)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    1-(5-phospho-beta-D-ribosyl)-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide.
    1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-AMP + diphosphate.
    L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.

    Cofactori

    Binds 1 zinc ion.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi660 – 6601ZincBy similarity
    Metal bindingi663 – 6631ZincBy similarity
    Active sitei729 – 7291By similarity
    Active sitei730 – 7301By similarity
    Metal bindingi764 – 7641ZincBy similarity
    Metal bindingi823 – 8231ZincBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. histidinol dehydrogenase activity Source: UniProtKB-EC
    3. NAD binding Source: InterPro
    4. phosphoribosyl-AMP cyclohydrolase activity Source: UniProtKB-EC
    5. phosphoribosyl-ATP diphosphatase activity Source: UniProtKB-EC
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. histidine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Hydrolase, Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesis

    Keywords - Ligandi

    ATP-binding, Metal-binding, NAD, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00031; UER00007.
    UPA00031; UER00008.
    UPA00031; UER00014.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidine biosynthesis trifunctional protein
    Including the following 3 domains:
    Phosphoribosyl-AMP cyclohydrolase (EC:3.5.4.19)
    Phosphoribosyl-ATP pyrophosphohydrolase (EC:3.6.1.31)
    Histidinol dehydrogenase (EC:1.1.1.23)
    Short name:
    HDH
    Gene namesi
    Name:HIS4
    OrganismiCandida albicans (Yeast)
    Taxonomic identifieri5476 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 838838Histidine biosynthesis trifunctional proteinPRO_0000135909Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliO74712.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 271271Phosphoribosyl-AMP cyclohydrolaseAdd
    BLAST
    Regioni272 – 36089Phosphoribosyl-ATP pyrophosphohydrolaseAdd
    BLAST
    Regioni361 – 838478Histidinol dehydrogenaseAdd
    BLAST

    Sequence similaritiesi

    In the C-terminal section; belongs to the histidinol dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG0141.

    Family and domain databases

    HAMAPiMF_01024. HisD.
    InterProiIPR016161. Ald_DH/histidinol_DH.
    IPR016298. Histidine_synth_trifunct.
    IPR001692. Histidinol_DH_CS.
    IPR012131. Hstdl_DH.
    IPR008179. PRib-ATP_PPHydrolase.
    IPR021130. PRib-ATP_PPHydrolase-like.
    IPR002496. PRib_AMP_CycHydrolase_dom.
    [Graphical view]
    PfamiPF00815. Histidinol_dh. 1 hit.
    PF01502. PRA-CH. 1 hit.
    PF01503. PRA-PH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001257. His_trifunctional. 1 hit.
    PRINTSiPR00083. HOLDHDRGNASE.
    ProDomiPD002610. PRA_CycHdrlase. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF53720. SSF53720. 1 hit.
    TIGRFAMsiTIGR00069. hisD. 1 hit.
    TIGR03188. histidine_hisI. 1 hit.
    PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O74712-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIFPILPVIS SPEDKQSIDE FSLVGQVLFP IESVSPKKHF IHQFPHDLDI    50
    FVNAIDNATT DQIVELLNVG IKQVFVNEKQ YHDAIEAGSP SSRFVVAVDV 100
    PSTELLTSEA SFVTSKPFSE SDLKKYNANE NRVIYIESNF TQDGAIELAK 150
    NYVPVIPSTK LTVKREEENK ISISAVFVST LTTDRPDGLY TTLITTPSPS 200
    YTALGIVYSS KDSIIAAIEE KVGVYQSRKR RDELWYKGKT SGATQKLVKL 250
    SKDCDSDVIQ FMVEPRTGYG FCHRETKFTC FGDDIADSPA RGLPKLDSTL 300
    QDRLENAPEG SYTKRLFDDE KLLIAKLKEE LDELIEAKSK EEIAWECADL 350
    VYFAMVWCIK HGVRLADIEK NLDVKSLKVS RRKGDAKPQY QEAPVNSSYK 400
    LEIVSVDDAA AVERAMTRPV QKTADIMKLV LPIIEKVKSD GDKALIELTS 450
    KFDGVKLDAP VLQAPFPADL MDISEEMKAA IDLSMQNIEK FHAAQLPKEK 500
    VMTVETSPGV YCSRFAKPIE NVGLYVPGGT AVLPSTAMML GVPAKVAGCK 550
    NIIVASPPSR ATGKLTPEVV YVAHKLGAKC IVMAGGAQAV TAMAYGTESV 600
    LKCDKILGPG NQFVTAAKMY VQNDTQALCS IDMPAGPSEV LVIADSNADA 650
    DFVASDLLSQ AEHGVDSQVI LIGVGLSDEK LNEFQAAVER QAKVLPRKDI 700
    VAKCLAHSYI LLAKTYKEAF DLSNQYAPEH LILQIDDAPS YVPDSIENAG 750
    SVFVGALSPE SCGDYSSGTN HTLPTYGYAR QYSGVNTATF QKFITSQEVT 800
    EKGLQNIGKA VMELARVEGL EAHRRAVEIR MERMAETK 838
    Length:838
    Mass (Da):91,836
    Last modified:November 1, 1998 - v1
    Checksum:iBFA0E97E9CA62C03
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ003115 Genomic DNA. Translation: CAA05871.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ003115 Genomic DNA. Translation: CAA05871.1 .

    3D structure databases

    ProteinModelPortali O74712.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0141.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00007 .
    UPA00031 ; UER00008 .
    UPA00031 ; UER00014 .

    Family and domain databases

    HAMAPi MF_01024. HisD.
    InterProi IPR016161. Ald_DH/histidinol_DH.
    IPR016298. Histidine_synth_trifunct.
    IPR001692. Histidinol_DH_CS.
    IPR012131. Hstdl_DH.
    IPR008179. PRib-ATP_PPHydrolase.
    IPR021130. PRib-ATP_PPHydrolase-like.
    IPR002496. PRib_AMP_CycHydrolase_dom.
    [Graphical view ]
    Pfami PF00815. Histidinol_dh. 1 hit.
    PF01502. PRA-CH. 1 hit.
    PF01503. PRA-PH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001257. His_trifunctional. 1 hit.
    PRINTSi PR00083. HOLDHDRGNASE.
    ProDomi PD002610. PRA_CycHdrlase. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF53720. SSF53720. 1 hit.
    TIGRFAMsi TIGR00069. hisD. 1 hit.
    TIGR03188. histidine_hisI. 1 hit.
    PROSITEi PS00611. HISOL_DEHYDROGENASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence of a 3.835 kbp DNA fragment containing the HIS4 gene and a fragment of a PEX5-like gene from Candida albicans."
      Navarro-Garcia F., Perez-Diaz R., Negredo A., Pla J., Nombela C.
      Yeast 14:1147-1157(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 64385 / 1001.

    Entry informationi

    Entry nameiHIS2_CANAX
    AccessioniPrimary (citable) accession number: O74712
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Multifunctional enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3