Reviewed, UniProtKB/Swiss-Prot O13471 (HIS2_KLULA)

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
Ordered Locus Names:	KLLA0C01452g

Organism

Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

28985 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	795 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	Complete proteome 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 – 795	795	Histidine biosynthesis trifunctional protein		PRO_0000135910
Regions
	Region	1 – 225	225	Phosphoribosyl-AMP cyclohydrolase
	Region	226 – 308	83	Phosphoribosyl-ATP pyrophosphohydrolase
	Region	309 – 795	487	Histidinol dehydrogenase
Sites
	Active site	683	1	By similarity
	Active site	684	1	By similarity
	Metal binding	614	1	Zinc By similarity
	Metal binding	617	1	Zinc By similarity
	Metal binding	717	1	Zinc By similarity
	Metal binding	776	1	Zinc By similarity
Experimental info
	Sequence conflict	162 – 163	2	VY → DI in CAA70698. Ref.1
	Sequence conflict	580 – 582	3	QAL → LAI in CAA70698. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O13471-1 [UniParc]. Last modified September 27, 2004. Version 2. Checksum: 6D35F1632280D3B3	FASTA	795	86,795
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The HIS4 gene from the yeast Kluyveromyces lactis." Freire-Picos M.A., Hampsey M., Cerdan M.E. Yeast 14:687-691(1998) [PubMed: 9639316] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.
[2]	"Genome evolution in yeasts." 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. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y09503 Genomic DNA. Translation: CAA70698.1. CR382123 Genomic DNA. Translation: CAH01111.1.
RefSeq	XP_452260.1.
3D structure databases
HSSP	HSSP built from PDB template 1K75 based on UniProtKB P06988.
ModBase	Search...
Genome annotation databases
GeneID	2892606.
KEGG	kla:KLLA0C01452g.
Phylogenomic databases
HOGENOM	O13471.
OMA	O13471. PESCGDY.
Enzyme and pathway databases
BRENDA	1.1.1.23. 74088. 3.5.4.19. 74088. 3.6.1.31. 74088.
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_KLULA

Accession

Primary (citable) accession number: O13471
Secondary accession number(s): Q6CUX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	September 27, 2004
Last modified:	June 16, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)