Reviewed, UniProtKB/Swiss-Prot O74712 (HIS2_CANAL)

Names and origin

Protein names

Recommended name:
    Histidine biosynthesis trifunctional protein
Including the following 3 domains:
    1- Recommended name:
            Phosphoribosyl-AMP cyclohydrolase
              EC=3.5.4.19
    2- Recommended name:
            Phosphoribosyl-ATP pyrophosphohydrolase
              EC=3.6.1.31
    3- Recommended name:
            Histidinol dehydrogenase
                Short name=HDH
              EC=1.1.1.23

Gene names

Name:

HIS4

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	838 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	1-(5-phosphoribosyl)-AMP + H(2)O = 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide. 1-(5-phosphoribosyl)-ATP + H(2)O = 1-(5-phosphoribosyl)-AMP + diphosphate. L-histidinol + 2 NAD(+) = L-histidine + 2 NADH.
Cofactor	Binds 1 zinc ion By similarity.
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	Metal-binding NAD Zinc
Molecular function	Hydrolase Oxidoreductase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activity Inferred from electronic annotation. Source: InterPro phosphoribosyl-AMP cyclohydrolase activity Inferred from electronic annotation. Source: InterPro phosphoribosyl-ATP diphosphatase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 838	838	Histidine biosynthesis trifunctional protein		PRO_0000135909
Regions
	Region	1 – 271	271	Phosphoribosyl-AMP cyclohydrolase
	Region	272 – 360	89	Phosphoribosyl-ATP pyrophosphohydrolase
	Region	361 – 838	478	Histidinol dehydrogenase
Sites
	Active site	729	1	By similarity
	Active site	730	1	By similarity
	Metal binding	660	1	Zinc By similarity
	Metal binding	663	1	Zinc By similarity
	Metal binding	764	1	Zinc By similarity
	Metal binding	823	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	O74712-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: BFA0E97E9CA62C03	FASTA	838	91,836
	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

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: 9778800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 64385 / 1001.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ003115 Genomic DNA. Translation: CAA05871.1.
3D structure databases
HSSP	HSSP built from PDB template 1K75 based on UniProtKB P06988.
ModBase	Search...
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]
PANTHER	PTHR21256:SF2. Hstdl_DH_prok. 1 hit.
Pfam	PF00815. Histidinol_dh. 1 hit. PF01502. PRA-CH. 1 hit. PF01503. PRA-PH. 1 hit. [Graphical view]
PIRSF	PIRSF001257. His_trifunctional. 1 hit.
PRINTS	PR00083. HOLDHDRGNASE.
ProDom	PD002680. Histidinol_dh. 1 hit. PD002610. PRA_cyclohydro. 1 hit. PD002611. Pra_PH/CH. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00069. hisD. 1 hit. TIGR03188. histidine_hisI. 1 hit.
PROSITE	PS00611. HISOL_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS2_CANAL

Accession

Primary (citable) accession number: O74712

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1998
Last modified:	November 25, 2008
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)