ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry O74712

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name HIS2_CANAL
Primary accession number O74712
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on November 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 51)
Name and origin of the protein
Protein name Histidine biosynthesis trifunctional protein
Synonyms None
Includes Phosphoribosyl-AMP cyclohydrolase
     (EC 3.5.4.19)
Phosphoribosyl-ATP pyrophosphohydrolase
     (EC 3.6.1.31)
Histidinol dehydrogenase
     (HDH)
     (EC 1.1.1.23)
Gene name
Name: HIS4
From
Candida albicans (Yeast) [TaxID: 5476] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; Candida.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 64385 / 1001;
DOI=10.1002/(SICI)1097-0061(19980915)14:12<1147::AID-YEA297>3.3.CO;2-Z; PubMed=9778800 [NCBI, ExPASy, EBI, Israel, Japan]
Navarro-Garcia F., Perez-Diaz R., Negredo A., Pla J., Nombela C.;
"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.";
Yeast 14:1147-1157(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ003115; CAA05871.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P06988; 1K75. [HSSP ENTRY / PDB]
ModBase O74712.
Ontologies
GO
GO:0004399; Molecular function: histidinol dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0004635; Molecular function: phosphoribosyl-AMP cyclohydrolase activity (inferred from electronic annotation from InterPro).
GO:0004636; Molecular function: phosphoribosyl-ATP diphosphatase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0000105; Biological process: histidine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016298; Histidine_synth_trifunct.
IPR001692; Histidinol_DHase.
IPR012131; Hstdl_DHase_prok.
IPR002496; PRA_CycOHase.
IPR008179; PRib-ATP_pyrophosphohydrolase.
Graphical view of domain structure.
PANTHER PTHR21256:SF2; Hstdl_DH_prok; 1.
Pfam PF00815; Histidinol_dh; 1.
PF01502; PRA-CH; 1.
PF01503; PRA-PH; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001257; His_trifunctional; 1.
PRINTS PR00083; HOLDHDRGNASE.
ProDom PD002680; Histidinol_dh; 1.
PD002610; PRA_cyclohydro; 1.
PD002611; Pra_PH/CH; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00069; hisD; 1.
TIGR03188; histidine_hisI; 1.
PROSITE PS00611; HISOL_DEHYDROGENASE; 1.
Other
ProtoNet O74712.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Histidine biosynthesis; Hydrolase; Metal-binding; Multifunctional enzyme; NAD; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   838  838     Histidine biosynthesis trifunctional protein. PRO_0000135909
REGION   1   271  271     Phosphoribosyl-AMP cyclohydrolase. 
REGION   272   360  89     Phosphoribosyl-ATP pyrophosphohydrolase. 
REGION   361   838  478     Histidinol dehydrogenase. 
ACT_SITE   729   729        By similarity. 
ACT_SITE   730   730        By similarity. 
METAL   660   660        Zinc (By similarity). 
METAL   663   663        Zinc (By similarity). 
METAL   764   764        Zinc (By similarity). 
METAL   823   823        Zinc (By similarity). 
Sequence information
Length: 838 AA [This is the length of the unprocessed precursor] Molecular weight: 91836 Da [This is the MW of the unprocessed precursor] CRC64: BFA0E97E9CA62C03 [This is a checksum on the sequence] 
        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
O74712 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by kr flag YPRC Korea Mirror sites: Australia Brazil Canada China Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!