Reviewed, UniProtKB/Swiss-Prot Q12670 (HIS2_SACBA)

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:

HIS2

Organism

Saccharomyces bayanus (Yeast) (Saccharomyces uvarum)

Taxonomic identifier

4931 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	799 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 + H2O = 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide. 1-(5-phosphoribosyl)-ATP + H2O = 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	ATP-binding Metal-binding NAD Nucleotide-binding Zinc
Molecular function	Hydrolase Oxidoreductase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW NAD or NADH binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activity Inferred from electronic annotation. Source: EC phosphoribosyl-AMP cyclohydrolase activity Inferred from electronic annotation. Source: EC phosphoribosyl-ATP diphosphatase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 799	799	Histidine biosynthesis trifunctional protein		PRO_0000135913
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

Sequences

	Sequence		Length	Mass (Da)
	Q12670-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 35793E26EDB81B6B	FASTA	799	87,734
	10 20 30 40 50 60 MVLPILPLID DLASWGTKKA YASLVGQVLL DGSSLNKDEV LQFAKEEEVP LVALSLPNAK 70 80 90 100 110 120 FSDDDIIAFL NNGVSSLFIA SQDAKIVDHL VEELNVPKNR IVVEGNGVFH NQFLVNQKFS 130 140 150 160 170 180 QDRIVSIKKL TKDLLIKEVV AEVRTDRPDG LFTTLVVDQY ERCLGLVYSS KESIAKAIDL 190 200 210 220 230 240 GRGVYYSRSR NEIWVKGETS GNGQKLLQIS TDCDSDALKF IVEQENVGFC HLETMSCFGE 250 260 270 280 290 300 FKHGLVGLES LLKQRLQDAP KESYTRRLFN DPALLDAKIK EEAEELTEAK GKQEISWEAA 310 320 330 340 350 360 DLFYFALAKL VTNNVSLKDV ENNLNMKHLK ITRRKGDAKP KFVAQAKAEE EAPTGPIHLH 370 380 390 400 410 420 VVNASDKEGI KKALSRPIQK TSEIMHLVNP IIENVRDRGD SALLEYTEKF DGVKLSTPVL 430 440 450 460 470 480 NAPFPEEYFE GLTEEMKDAL DLSIENVRKF HAAQLPKETL EVETQPGVLC SRFPRPIEKV 490 500 510 520 530 540 GLYIPGGTAI LPSTALMLGV PAQVAQCKEI VFASPPRKSD GKVSPEVVYV AEKVGARMIV 550 560 570 580 590 600 LAGGAQAVAA MAYGTETIPK VDKVLGPGNQ FVTAAKMYVQ NDTQALCSID MPAGPSEVLV 610 620 630 640 650 660 IADEDADADF VASDLLSQAE HGIDSQVILV GIKLSEKKIQ EIQDAVHDQA MQLPRVDIVR 670 680 690 700 710 720 KCIAHSTIIL CDGYEEALEM SNKYAPEHLI LQIANANDYV KLVDNAGSVF VGAYTPESCG 730 740 750 760 770 780 DYSSGTNHTL PTYGYARQYS GANTATFQKF ITAQNITPEG LENIGRAVMC VAKKEGLDGH 790 RNAVKIRMSK LGLIPKDFQ

References

[1]	Porter G.L. Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Carlsbergensis.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U13062 Genomic DNA. Translation: AAA21153.1.
PIR	S53349.
3D structure databases
HSSP	HSSP built from PDB template 1K75 based on UniProtKB P06988.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.23. 164752. 3.5.4.19. 164752. 3.6.1.31. 164752.
Family and domain databases
InterPro	IPR016298. Histidine_synth_trifunct. IPR001692. Histidinol_DH_CS. IPR012131. Hstdl_DH_prok-type. IPR002496. PRA_CycHdrlase. 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_SACBA

Accession

Primary (citable) accession number: Q12670

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)