Q6CID6 (HIS1_KLULA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP phosphoribosyltransferase
Short name=ATP-PRT
Short name=ATP-PRTase
EC=2.4.2.17

Gene names

Name:	HIS1
Ordered Locus Names:	KLLA0F27489g

Organism

Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

284590 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces › Kluyveromyces lactis

Protein attributes

Sequence length	297 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of the enzymatic activity By similarity.
Catalytic activity	1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate.
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the ATP phosphoribosyltransferase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP phosphoribosyltransferase activity Inferred from electronic annotation. Source: EC magnesium 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 – 297	297	ATP phosphoribosyltransferase		PRO_0000151955

Sequences

	Sequence		Length	Mass (Da)
	Q6CID6 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: F471B9D3E7B907F6	FASTA	297	32,315
	10 20 30 40 50 60 MDLVNHLNDK LLFAIPKKGR LYEKSVSILK GSDIKFHRSA RLDIAISTNM PVALIFLPAA 70 80 90 100 110 120 DIPMFVGEGR CDLGITGVDQ VRESEVDVNL PIDLQFGTCK LQVQVPVAGE YTSPEQLIGK 130 140 150 160 170 180 TIVSSFVNLT KKYFAQLEGV PESEMVTRVK YVGGSVEASC ALGVADAIVD LVESGETMRA 190 200 210 220 230 240 AGLTAIATVL DTSAHLIESK NPKGDVELLR TIKSRIEGVM TAQKYVSCSY NAPENKLPEL 250 260 270 280 290 LKITPGRRAP TISQINDSGW VAVSSMIERK NKGDIMDDLK KNGAEDIMVF EISNCRV

References

[1]

"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382126 Genomic DNA. Translation: CAG99011.1.
RefSeq	XP_456303.1. XM_456303.1.
3D structure databases
ProteinModelPortal	Q6CID6.
ModBase	Search...
Protein-protein interaction databases
STRING	28985.Q6CID6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2894810.
KEGG	kla:KLLA0F27489g.
Phylogenomic databases
eggNOG	COG0040.
HOGENOM	HOG000223250.
KO	K00765.
OMA	EGKHIAT.
OrthoDB	EOG4K9FN2.
Enzyme and pathway databases
UniPathway	UPA00031; UER00006.
Family and domain databases
Gene3D	3.30.70.120. 1 hit.
InterPro	IPR013820. ATP_PRibTrfase_cat. IPR018198. ATP_PRibTrfase_CS. IPR001348. ATP_PRibTrfase_HisG. IPR020621. ATP_PRibTrfase_HisG_long. IPR013115. HisG_C. IPR011322. N-reg_PII-like_a/b. IPR015867. N-reg_PII/ATP_PRibTrfase_C. [Graphical view]
PANTHER	PTHR21403. PTHR21403. 1 hit.
Pfam	PF01634. HisG. 1 hit. PF08029. HisG_C. 1 hit. [Graphical view]
SUPFAM	SSF54913. N-reg_PII-like_a/b. 1 hit.
TIGRFAMs	TIGR00070. hisG. 1 hit. TIGR03455. HisG_C-term. 1 hit.
PROSITE	PS01316. ATP_P_PHORIBOSYLTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS1_KLULA

Accession

Primary (citable) accession number: Q6CID6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	August 16, 2004
Last modified:	May 29, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program