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
	OrderedLocusNames:	KLLA0C01452g

From

Kluyveromyces lactis (Yeast) (Candida sphaerica)

[TaxID: 28985]

Taxonomy

Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
DOI=10.1002/(SICI)1097-0061(199805)14:7<687::AID-YEA261>3.0.CO;2-4; PubMed=9639316 [NCBI, ExPASy, EBI, Israel, Japan]
Freire-Picos M.A., Hampsey M., Cerdan M.E.;
"The HIS4 gene from the yeast Kluyveromyces lactis.";
Yeast 14:687-691(1998).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).

Comments

CATALYTIC ACTIVITY: 1-(5-phosphoribosyl)-AMP + H₂O = 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide.
CATALYTIC ACTIVITY: 1-(5-phosphoribosyl)-ATP + H₂O = 1-(5-phosphoribosyl)-AMP + diphosphate.
CATALYTIC ACTIVITY: 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 .
PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9 .
PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9 .
SIMILARITY: In the C-terminal section; belongs to the histidinol dehydrogenase family.

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

Y09503; CAA70698.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR382123; CAH01111.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_452260.1; -.

3D structure databases

HSSP

P06988; 1K75. [HSSP ENTRY / PDB]

ModBase

O13471.

Ontologies

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.

Genome annotation databases

GeneID

2892606; -.

KEGG

kla:KLLA0C01452g; -.

Phylogenomic databases

HOGENOM

O13471; -.

Other

ProtoNet

O13471.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; Hydrolase; Metal-binding; Multifunctional enzyme; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 795`	`795`	`Histidine biosynthesis trifunctional protein.`	`PRO_0000135910`
`REGION`	`1 225`	`225`	`Phosphoribosyl-AMP cyclohydrolase.`
`REGION`	`226 308`	`83`	`Phosphoribosyl-ATP pyrophosphohydrolase.`
`REGION`	`309 795`	`487`	`Histidinol dehydrogenase.`
`ACT_SITE`	`683 683`		`By similarity.`
`ACT_SITE`	`684 684`		`By similarity.`
`METAL`	`614 614`		`Zinc (By similarity).`
`METAL`	`617 617`		`Zinc (By similarity).`
`METAL`	`717 717`		`Zinc (By similarity).`
`METAL`	`776 776`		`Zinc (By similarity).`
`CONFLICT`	`162 163`		`VY -> DI (in Ref. 1; CAA70698).`
`CONFLICT`	`580 582`		`QAL -> LAI (in Ref. 1; CAA70698).`

Sequence information

Length: 795 AA [This is the length of the unprocessed precursor]

Molecular weight: 86795 Da [This is the MW of the unprocessed precursor]

CRC64: 6D35F1632280D3B3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLPVVPVFNA VNALKEKTYL YLSSQLVLDG KDMTKDDILE FVQNSHGQNI SVLLKDAKFE 

        70         80         90        100        110        120 
DDDLIVLLNN GVVTLFIDSD DYAAHLVEIG VPSIRLTLLK DGAYQFSFGQ IQEIQQSQLV 

       130        140        150        160        170        180 
KASEISLETF TNSVLSGMKT DRPDGLYTTL VVDENERSLG LVYSNKESVS LAIETQTGIY 

       190        200        210        220        230        240 
FSRSRNEIWR KGATSGNVQK LLSIELDCDG DALKFVVRQG GSGSFCHLET ESCFGNFRHG 

       250        260        270        280        290        300 
LYGLQKLLQE RLLNAPEGSY TKRLFNDSDL LTAKIKEEAE ELTEAVDKKD IAWECADLFY 

       310        320        330        340        350        360 
FAMARLVANG VSLEDVERNL NTKHLKITRR KGDAKPKFLK KEPVAVHEED GKIVLNVVSA 

       370        380        390        400        410        420 
SDKAAVEKAV TRPIQKTAEI MNLVNPIIEN VIKNGDKALV ELTAKFDGVQ LETPVLEAPY 

       430        440        450        460        470        480 
PEEYLDGLTD ELRDALDLSI ENVKKFHAAQ MQSETLDVET QPGVVCSRFP RPIEKVGLYI 

       490        500        510        520        530        540 
PGGTAILPST ALMLGVPAQV AGCKEIVFAS PPRKSDGRVS PEVVYVASKV GASKIVLAGG 

       550        560        570        580        590        600 
AQAIAAMAYG TESVPKVDKI LGPGNQFVTA AKMYVQNDTQ ALCSIDMPAG PSEVLVICDE 

       610        620        630        640        650        660 
EADVDFVASD LLSQAEHGID SQVILVGVSL SDSKIEALQN AVHEQAMQLP RVDIVRKCIA 

       670        680        690        700        710        720 
HSSIILCDSY EEAFKMSNQY APEHLILQIS NAEDYVKDVD HAGSIFVGAY TPESCGDYSS 

       730        740        750        760        770        780 
GTNHTLPTYG YARQYSGVNT ATFQKFITSQ VVTPVGLEHI GHAVMSVAKV EGLDAHRNAV 

       790 
KIRMSKLGLL PSGFE

O13471 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 submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools