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Protein

Histidine biosynthesis trifunctional protein

Gene

HIS4

Organism
Candida albicans (Yeast)
Status
Reviewed-Annotation score: 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.
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

Zn2+By similarityNote: Binds 1 zinc ion.By similarity

Pathway:iL-histidine biosynthesis

This protein is involved in step 2, 3 and 9 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Histidine biosynthesis trifunctional protein (HIS4)
  3. Histidine biosynthesis trifunctional protein (HIS4)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (HIS6)
  5. no protein annotated in this organism
  6. Imidazoleglycerol-phosphate dehydratase (HIS3)
  7. no protein annotated in this organism
  8. no protein annotated in this organism
  9. Histidine biosynthesis trifunctional protein (HIS4)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

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

GO - Biological processi

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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

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

        10         20         30         40         50
MIFPILPVIS SPEDKQSIDE FSLVGQVLFP IESVSPKKHF IHQFPHDLDI
60 70 80 90 100
FVNAIDNATT DQIVELLNVG IKQVFVNEKQ YHDAIEAGSP SSRFVVAVDV
110 120 130 140 150
PSTELLTSEA SFVTSKPFSE SDLKKYNANE NRVIYIESNF TQDGAIELAK
160 170 180 190 200
NYVPVIPSTK LTVKREEENK ISISAVFVST LTTDRPDGLY TTLITTPSPS
210 220 230 240 250
YTALGIVYSS KDSIIAAIEE KVGVYQSRKR RDELWYKGKT SGATQKLVKL
260 270 280 290 300
SKDCDSDVIQ FMVEPRTGYG FCHRETKFTC FGDDIADSPA RGLPKLDSTL
310 320 330 340 350
QDRLENAPEG SYTKRLFDDE KLLIAKLKEE LDELIEAKSK EEIAWECADL
360 370 380 390 400
VYFAMVWCIK HGVRLADIEK NLDVKSLKVS RRKGDAKPQY QEAPVNSSYK
410 420 430 440 450
LEIVSVDDAA AVERAMTRPV QKTADIMKLV LPIIEKVKSD GDKALIELTS
460 470 480 490 500
KFDGVKLDAP VLQAPFPADL MDISEEMKAA IDLSMQNIEK FHAAQLPKEK
510 520 530 540 550
VMTVETSPGV YCSRFAKPIE NVGLYVPGGT AVLPSTAMML GVPAKVAGCK
560 570 580 590 600
NIIVASPPSR ATGKLTPEVV YVAHKLGAKC IVMAGGAQAV TAMAYGTESV
610 620 630 640 650
LKCDKILGPG NQFVTAAKMY VQNDTQALCS IDMPAGPSEV LVIADSNADA
660 670 680 690 700
DFVASDLLSQ AEHGVDSQVI LIGVGLSDEK LNEFQAAVER QAKVLPRKDI
710 720 730 740 750
VAKCLAHSYI LLAKTYKEAF DLSNQYAPEH LILQIDDAPS YVPDSIENAG
760 770 780 790 800
SVFVGALSPE SCGDYSSGTN HTLPTYGYAR QYSGVNTATF QKFITSQEVT
810 820 830
EKGLQNIGKA VMELARVEGL EAHRRAVEIR MERMAETK
Length:838
Mass (Da):91,836
Last modified:November 1, 1998 - v1
Checksum:iBFA0E97E9CA62C03
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ003115 Genomic DNA. Translation: CAA05871.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ003115 Genomic DNA. Translation: CAA05871.1.

3D structure databases

ProteinModelPortaliO74712.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG0141.

Enzyme and pathway databases

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

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]
ProtoNetiSearch...

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: November 26, 2014
This is version 87 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.