Reviewed, UniProtKB/Swiss-Prot P45353 (HIS2_PICPA)

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

Pichia pastoris (Yeast)

Taxonomic identifier

4922 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Pichia

Protein attributes

Sequence length	842 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 – 842	842	Histidine biosynthesis trifunctional protein		PRO_0000135912
Regions
	Region	1 – 275	275	Phosphoribosyl-AMP cyclohydrolase
	Region	276 – 357	82	Phosphoribosyl-ATP pyrophosphohydrolase
	Region	358 – 842	485	Histidinol dehydrogenase
Sites
	Active site	736	1	By similarity
	Active site	737	1	By similarity
	Metal binding	667	1	Zinc By similarity
	Metal binding	670	1	Zinc By similarity
	Metal binding	769	1	Zinc By similarity
	Metal binding	828	1	Zinc By similarity
Experimental info
	Sequence conflict	92	1	R → RM Ref.2
	Sequence conflict	507	1	A → T in CAA39641. Ref.2
	Sequence conflict	661	1	V → A in CAA39641. Ref.2
	Sequence conflict	746	1	S → SS in CAA39641. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P45353-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 67DA24E2266A4A3E	FASTA	842	91,942
	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

References

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	U14126 Genomic DNA. Translation: AAA67001.1. X56180 Genomic DNA. Translation: CAA39641.1.
PIR	S51513.
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_PICPA

Accession

Primary (citable) accession number: P45353

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 25, 2008
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)