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

Pichia pastoris (Yeast)

[TaxID: 4922]

Taxonomy

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

Protein existence

3: Inferred from homology;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/BF00309932; PubMed=7874737 [NCBI, ExPASy, EBI, Israel, Japan] Crane D.I., Gould S.J.; "The Pichia pastoris HIS4 gene: nucleotide sequence, creation of a non-reverting his4 deletion mutant, and development of HIS4-based replicating and integrating plasmids."; Curr. Genet. 26:443-450(1994).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=NRRL Y-11430; Koutz P.J., Davis G.R., Thill G.P.; Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases.

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

U14126; AAA67001.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X56180; CAA39641.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S51513; S51513.

3D structure databases

HSSP

P06988; 1K75. [HSSP ENTRY / PDB]

ModBase

P45353.

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

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

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 842`	`842`	`Histidine biosynthesis trifunctional protein.`	`PRO_0000135912`
`REGION`	`1 275`	`275`	`Phosphoribosyl-AMP cyclohydrolase.`
`REGION`	`276 357`	`82`	`Phosphoribosyl-ATP pyrophosphohydrolase.`
`REGION`	`358 842`	`485`	`Histidinol dehydrogenase.`
`ACT_SITE`	`736 736`		`By similarity.`
`ACT_SITE`	`737 737`		`By similarity.`
`METAL`	`667 667`		`Zinc (By similarity).`
`METAL`	`670 670`		`Zinc (By similarity).`
`METAL`	`769 769`		`Zinc (By similarity).`
`METAL`	`828 828`		`Zinc (By similarity).`
`CONFLICT`	`92 92`		`R -> RM (in Ref. 2).`
`CONFLICT`	`507 507`		`A -> T (in Ref. 2; CAA39641).`
`CONFLICT`	`661 661`		`V -> A (in Ref. 2; CAA39641).`
`CONFLICT`	`746 746`		`S -> SS (in Ref. 2; CAA39641).`

Sequence information

Length: 842 AA [This is the length of the unprocessed precursor]

Molecular weight: 91942 Da [This is the MW of the unprocessed precursor]

CRC64: 67DA24E2266A4A3E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTFPLLPAYA SVAEFDNSLS LVGKAVFPYA ADQLHNLIKF TQSTELQVNV QVESSVTEDQ 

        70         80         90        100        110        120 
FEELIDNLLK LYNNGINEVI LDLDLAERVV QRIPGARVIY RTLVDKVASL PANASIAVPF 

       130        140        150        160        170        180 
SSPLGDLKSF TNGGSRTVYA FSETAKLVDV TSTVASGIIP IIDARQLTTE YELSEDVKKF 

       190        200        210        220        230        240 
PVSEILLASL TTDRPDGLFT TLVADSSNYS LGLVYSSKKS IPEAIRTQTG VYQSRRHGLW 

       250        260        270        280        290        300 
YKGATSGATQ KLLGIELDCD GDCLKFVVEQ TGVGFCHLER TSCFGQSKGL RAMEATLWDR 

       310        320        330        340        350        360 
KSNAPEGSYT KRLFDDEVLL NAKIREEADE LAEAKSKEDI AWECADLFYF ALVRCAKYGV 

       370        380        390        400        410        420 
TLDEVERNLD MKSLKVTRRK GDAKPGYTKE QPKEESKPKE VPSEGRIELC KIDVSKASSQ 

       430        440        450        460        470        480 
EIEDALRRPI QKTEQIMELV KPIVDNVRQN GDKALLELTA KFDGVALKTP VLEAPFPEEL 

       490        500        510        520        530        540 
MQLPDNVKRA IDLSIDNVRK FHEAQLAETL QVETCPGVVC SRFARPIEKV GLYIPGGTAI 

       550        560        570        580        590        600 
LPSTSLMLGV PAKVAGCKEI VFASPPKKDG TLTPEVIYVA HKVGAKCIVL AGGAQAVAAM 

       610        620        630        640        650        660 
AYGTETVPKC DKIFGPGNQF VTAAKMMVQN DTSALCSIDM PAGPSEVLVI ADKYADPDFV 

       670        680        690        700        710        720 
VSDLLSQAEH GIDSQVILLA VDMTDKELAR IEDAVHNQAV QLPRVEIVRK CIAHSTTLSV 

       730        740        750        760        770        780 
ATYEQALEMS NQYAPEHLIL QIENASYVDQ VQHAGSVFVG AYSPESCGDY SSGTNHTLPT 

       790        800        810        820        830        840 
YGYARQYSGV NTATFQKFIT SQDVTPEGLK HIGQAVMDLA AVEGLDAHRN AVKVRMEKLG 


LI

P45353 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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