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O74712

- HIS2_CANAX

UniProt

O74712 - HIS2_CANAX

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Protein
Histidine biosynthesis trifunctional protein
Gene
HIS4
Organism
Candida albicans (Yeast)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

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.UniRule annotation
1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-AMP + diphosphate.UniRule annotation
L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.UniRule annotation

Cofactori

Binds 1 zinc ion By similarity.UniRule annotation

Pathwayi

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. histidine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

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 proteinUniRule annotation
PRO_0000135909Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliO74712.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 271271Phosphoribosyl-AMP cyclohydrolaseUniRule annotation
Add
BLAST
Regioni272 – 36089Phosphoribosyl-ATP pyrophosphohydrolaseUniRule annotation
Add
BLAST
Regioni361 – 838478Histidinol dehydrogenaseUniRule annotation
Add
BLAST

Sequence similaritiesi

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

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...

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: February 19, 2014
This is version 84 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

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