Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O74712 (HIS2_CANAX) 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:
Histidine biosynthesis trifunctional protein

Including the following 3 domains:

  1. Phosphoribosyl-AMP cyclohydrolase
    EC=3.5.4.19
  2. Phosphoribosyl-ATP pyrophosphohydrolase
    EC=3.6.1.31
  3. Histidinol dehydrogenase
    Short name=HDH
    EC=1.1.1.23
Gene names
Name:HIS4
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length838 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

1-(5-phospho-beta-D-ribosyl)-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide. HAMAP-Rule MF_01024

1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-AMP + diphosphate. HAMAP-Rule MF_01024

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP-Rule MF_01024

Cofactor

Binds 1 zinc ion By similarity. HAMAP-Rule MF_01024

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. HAMAP-Rule MF_01024

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 838838Histidine biosynthesis trifunctional protein HAMAP-Rule MF_01024
PRO_0000135909

Regions

Region1 – 271271Phosphoribosyl-AMP cyclohydrolase HAMAP-Rule MF_01024
Region272 – 36089Phosphoribosyl-ATP pyrophosphohydrolase HAMAP-Rule MF_01024
Region361 – 838478Histidinol dehydrogenase HAMAP-Rule MF_01024

Sites

Active site7291 By similarity
Active site7301 By similarity
Metal binding6601Zinc By similarity
Metal binding6631Zinc By similarity
Metal binding7641Zinc By similarity
Metal binding8231Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
O74712 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: BFA0E97E9CA62C03

FASTA83891,836
        10         20         30         40         50         60 
MIFPILPVIS SPEDKQSIDE FSLVGQVLFP IESVSPKKHF IHQFPHDLDI FVNAIDNATT 

        70         80         90        100        110        120 
DQIVELLNVG IKQVFVNEKQ YHDAIEAGSP SSRFVVAVDV PSTELLTSEA SFVTSKPFSE 

       130        140        150        160        170        180 
SDLKKYNANE NRVIYIESNF TQDGAIELAK NYVPVIPSTK LTVKREEENK ISISAVFVST 

       190        200        210        220        230        240 
LTTDRPDGLY TTLITTPSPS YTALGIVYSS KDSIIAAIEE KVGVYQSRKR RDELWYKGKT 

       250        260        270        280        290        300 
SGATQKLVKL SKDCDSDVIQ FMVEPRTGYG FCHRETKFTC FGDDIADSPA RGLPKLDSTL 

       310        320        330        340        350        360 
QDRLENAPEG SYTKRLFDDE KLLIAKLKEE LDELIEAKSK EEIAWECADL VYFAMVWCIK 

       370        380        390        400        410        420 
HGVRLADIEK NLDVKSLKVS RRKGDAKPQY QEAPVNSSYK LEIVSVDDAA AVERAMTRPV 

       430        440        450        460        470        480 
QKTADIMKLV LPIIEKVKSD GDKALIELTS KFDGVKLDAP VLQAPFPADL MDISEEMKAA 

       490        500        510        520        530        540 
IDLSMQNIEK FHAAQLPKEK VMTVETSPGV YCSRFAKPIE NVGLYVPGGT AVLPSTAMML 

       550        560        570        580        590        600 
GVPAKVAGCK NIIVASPPSR ATGKLTPEVV YVAHKLGAKC IVMAGGAQAV TAMAYGTESV 

       610        620        630        640        650        660 
LKCDKILGPG NQFVTAAKMY VQNDTQALCS IDMPAGPSEV LVIADSNADA DFVASDLLSQ 

       670        680        690        700        710        720 
AEHGVDSQVI LIGVGLSDEK LNEFQAAVER QAKVLPRKDI VAKCLAHSYI LLAKTYKEAF 

       730        740        750        760        770        780 
DLSNQYAPEH LILQIDDAPS YVPDSIENAG SVFVGALSPE SCGDYSSGTN HTLPTYGYAR 

       790        800        810        820        830 
QYSGVNTATF QKFITSQEVT EKGLQNIGKA VMELARVEGL EAHRRAVEIR MERMAETK 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ003115 Genomic DNA. Translation: CAA05871.1.

3D structure databases

ProteinModelPortalO74712.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0141.

Enzyme and pathway databases

UniPathwayUPA00031; UER00007.
UPA00031; UER00008.
UPA00031; UER00014.

Family and domain databases

HAMAPMF_01024. HisD.
InterProIPR016161. 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]
PfamPF00815. Histidinol_dh. 1 hit.
PF01502. PRA-CH. 1 hit.
PF01503. PRA-PH. 1 hit.
[Graphical view]
PIRSFPIRSF001257. His_trifunctional. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
ProDomPD002610. PRA_CycHdrlase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
TIGR03188. histidine_hisI. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHIS2_CANAX
AccessionPrimary (citable) accession number: O74712
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: February 19, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways