P00815 (HIS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidine biosynthesis trifunctional protein

Including the following 3 domains:

1. Phosphoribosyl-AMP cyclohydrolase
   EC=3.5.4.19
2. Phosphoribosyl-ATP pyrophosphohydrolase
   EC=3.6.1.31
3. Histidinol dehydrogenase
   Short name=HDH
   EC=1.1.1.23

Gene names

Name:	HIS4
Ordered Locus Names:	YCL030C
ORF Names:	YCL30C, YCL183

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	799 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	1-(5-phosphoribosyl)-AMP + H2O = 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide. 1-(5-phosphoribosyl)-ATP + H2O = 1-(5-phosphoribosyl)-AMP + diphosphate. L-histidinol + H2O + 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.
Miscellaneous	Present with 521 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	In the C-terminal section; belongs to the histidinol dehydrogenase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	ATP-binding Metal-binding NAD Nucleotide-binding Zinc
Molecular function	Hydrolase Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from mutant phenotype. Source: SGD
Cellular component	intracellular Traceable author statement. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW NAD binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activity Inferred from direct assay. Source: SGD phosphoribosyl-AMP cyclohydrolase activity Inferred from direct assay. Source: SGD phosphoribosyl-ATP diphosphatase activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FMP48	P53233	4	EBI-8334,EBI-9664

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 799	799	Histidine biosynthesis trifunctional protein		PRO_0000135914
Regions
	Region	1 – 229	229	Phosphoribosyl-AMP cyclohydrolase
	Region	230 – 312	83	Phosphoribosyl-ATP pyrophosphohydrolase
	Region	313 – 799	487	Histidinol dehydrogenase
Sites
	Active site	687	1	By similarity
	Active site	688	1	By similarity
	Metal binding	618	1	Zinc By similarity
	Metal binding	621	1	Zinc By similarity
	Metal binding	721	1	Zinc By similarity
	Metal binding	780	1	Zinc By similarity
Amino acid modifications
	Modified residue	265	1	Phosphothreonine Ref.9
Experimental info
	Sequence conflict	53	1	A → R in CAA24617. Ref.1
	Sequence conflict	386	1	H → Y in CAA24617. Ref.1
	Sequence conflict	402 – 403	2	AL → VF in CAA24617. Ref.1
	Sequence conflict	441	1	D → N in CAA24617. Ref.1
	Sequence conflict	794	1	I → F in CAA24617. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P00815 [UniParc]. Last modified March 29, 2004. Version 3. Checksum: 0B82D289BEAB754D	FASTA	799	87,721
	10 20 30 40 50 60 MVLPILPLID DLASWNSKKE YVSLVGQVLL DGSSLSNEEI LQFSKEEEVP LVALSLPSGK 70 80 90 100 110 120 FSDDEIIAFL NNGVSSLFIA SQDAKTAEHL VEQLNVPKER VVVEENGVFS NQFMVKQKFS 130 140 150 160 170 180 QDKIVSIKKL SKDMLTKEVL GEVRTDRPDG LYTTLVVDQY ERCLGLVYSS KKSIAKAIDL 190 200 210 220 230 240 GRGVYYSRSR NEIWIKGETS GNGQKLLQIS TDCDSDALKF IVEQENVGFC HLETMSCFGE 250 260 270 280 290 300 FKHGLVGLES LLKQRLQDAP EESYTRRLFN DSALLDAKIK EEAEELTEAK GKKELSWEAA 310 320 330 340 350 360 DLFYFALAKL VANDVSLKDV ENNLNMKHLK VTRRKGDAKP KFVGQPKAEE EKLTGPIHLD 370 380 390 400 410 420 VVKASDKVGV QKALSRPIQK TSEIMHLVNP IIENVRDKGN SALLEYTEKF DGVKLSNPVL 430 440 450 460 470 480 NAPFPEEYFE GLTEEMKEAL DLSIENVRKF HAAQLPTETL EVETQPGVLC SRFPRPIEKV 490 500 510 520 530 540 GLYIPGGTAI LPSTALMLGV PAQVAQCKEI VFASPPRKSD GKVSPEVVYV AEKVGASKIV 550 560 570 580 590 600 LAGGAQAVAA MAYGTETIPK VDKILGPGNQ FVTAAKMYVQ NDTQALCSID MPAGPSEVLV 610 620 630 640 650 660 IADEDADVDF VASDLLSQAE HGIDSQVILV GVNLSEKKIQ EIQDAVHNQA LQLPRVDIVR 670 680 690 700 710 720 KCIAHSTIVL CDGYEEALEM SNQYAPEHLI LQIANANDYV KLVDNAGSVF VGAYTPESCG 730 740 750 760 770 780 DYSSGTNHTL PTYGYARQYS GANTATFQKF ITAQNITPEG LENIGRAVMC VAKKEGLDGH 790 RNAVKIRMSK LGLIPKDFQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of the HIS4 region of yeast." Donahue T.F., Farabaugh P.J., Fink G.R. Gene 18:47-59(1982) [PubMed: 7049842] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"The complete sequence of a 11,953 bp fragment from C1G on chromosome III encompasses four new open reading frames." Rad M.R., Luetzenkirchen K., Xu G., Kleinhans U., Hollenberg C.P. Yeast 7:533-538(1991) [PubMed: 1897318] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[3]	"The complete DNA sequence of yeast chromosome III." Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G. Nature 357:38-46(1992) [PubMed: 1574125] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Valles G., Volckaerts G. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 375.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Insertion of the eukaryotic transposable element Ty1 creates a 5-base pair duplication." Farabaugh P.J., Fink G.R. Nature 286:352-356(1980) [PubMed: 6250062] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-20.
[7]	"Transposable element sequences involved in the enhancement of yeast gene expression." Roeder G.S., Rose A.B., Pearlman R.E. Proc. Natl. Acad. Sci. U.S.A. 82:5428-5432(1985) [PubMed: 2991923] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-265, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	V01310 Genomic DNA. Translation: CAA24617.1. X59720 Genomic DNA. Translation: CAA42355.2. V01309 Genomic DNA. Translation: CAA24616.1. M11491 Genomic DNA. Translation: AAA67504.1. M11492 Genomic DNA. Translation: AAA67505.1. M11694 Unassigned DNA. Translation: AAA18400.1. M11695 Unassigned DNA. Translation: AAA18401.1. M11696 Unassigned DNA. Translation: AAA18402.1. BK006937 Genomic DNA. Translation: DAA07454.1.
PIR	SHBY. S17473.
RefSeq	NP_009900.2. NM_001178675.1.
3D structure databases
ProteinModelPortal	P00815.
SMR	P00815. Positions 142-241, 247-324, 363-793.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6402N.
IntAct	P00815. 16 interactions.
MINT	MINT-617364.
STRING	P00815.
Proteomic databases
PeptideAtlas	P00815.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YCL030C; YCL030C; YCL030C.
GeneID	850327.
KEGG	sce:YCL030C.
NMPDR	fig|4932.3.peg.620.
Organism-specific databases
CYGD	YCL030c.
SGD	S000000535. HIS4.
Phylogenomic databases
eggNOG	fuNOG06008.
GeneTree	EFGT00050000001873.
HOGENOM	HBG329596.
OMA	LGPGNQF.
OrthoDB	EOG44N216.
Gene expression databases
ArrayExpress	P00815.
Genevestigator	P00815.
GermOnline	YCL030C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR016298. Histidine_synth_trifunct. IPR001692. Histidinol_DH_CS. IPR012131. Hstdl_DH. IPR008179. PRib-ATP_PPHydrolase. IPR021130. PRib-ATP_PPHydrolase-like. IPR002496. PRib_AMP_CycHydrolase. [Graphical view]
KO	K14152.
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	PD002610. PRA_CycHdrlase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMs	TIGR00069. HisD. 1 hit. TIGR03188. Histidine_hisI. 1 hit.
PROSITE	PS00611. HISOL_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	965751.

Entry information

Entry name

HIS2_YEAST

Accession

Primary (citable) accession number: P00815
Secondary accession number(s): D6VQY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	March 29, 2004
Last modified:	December 14, 2011
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program