Q8P9P3 (HIS1_XANCP) 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:	hisG
Ordered Locus Names:	XCC1808

Organism

Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568) [Reference proteome] [HAMAP]

Taxonomic identifier

190485 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas › Xanthomonas campestris › Xanthomonas campestris pv. campestris

Protein attributes

Sequence length	304 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 HisG enzymatic activity By similarity. HAMAP-Rule MF_00079
Catalytic activity	1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00079
Cofactor	Magnesium By similarity.
Enzyme regulation	Feedback inhibited by histidine By similarity. HAMAP-Rule MF_00079
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. HAMAP-Rule MF_00079
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the ATP phosphoribosyltransferase family. Long subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
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: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 304	304	ATP phosphoribosyltransferase HAMAP-Rule MF_00079		PRO_0000151874

Sequences

	Sequence		Length	Mass (Da)
	Q8P9P3 [UniParc]. Last modified October 10, 2002. Version 1. Checksum: 66D10687E96308F2	FASTA	304	32,676
	10 20 30 40 50 60 MSASTAAPAR DRLRIAIQKN GRLAEPARSL LAACGLSWRQ SRDKLFCYGE SLPVDLLLVR 70 80 90 100 110 120 DDDIPGLIAD GVCDLGIVGQ NELDEQASAR RRAGLPAAYH AVRGVGFGQC RLMLAVPEEW 130 140 150 160 170 180 GWQGVAQLAG KRIATSYPAI LADWLERQGI DASVVELSGS VEIAPRLGTA DLICDLVSSG 190 200 210 220 230 240 ATLAANQLKP VELVMESEAV LAGAVREPAD ARAALLAMLL RRMDGVLKLR DSKLLMFRAE 250 260 270 280 290 300 QGNVDALRRL LPDADPLVQL PDDGNGALRL QTMCHGAVTW QRLEELERAG AQGLMVLTVE RSLA

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33913 / NCPPB 528 / LMG 568.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008922 Genomic DNA. Translation: AAM41097.1.
RefSeq	NP_637173.1. NC_003902.1.
3D structure databases
ProteinModelPortal	Q8P9P3.
ModBase	Search...
Protein-protein interaction databases
STRING	190485.XCC1808.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM41097; AAM41097; XCC1808.
GeneID	998451.
KEGG	xcc:XCC1808.
PATRIC	24074441. VBIXanCam115730_1928.
Phylogenomic databases
eggNOG	COG0040.
HOGENOM	HOG000223247.
KO	K00765.
OMA	EGKHIAT.
ProtClustDB	PRK00489.
Enzyme and pathway databases
UniPathway	UPA00031; UER00006.
Family and domain databases
HAMAP	MF_00079. HisG_Long.
InterPro	IPR013820. ATP_PRibTrfase_cat. IPR018198. ATP_PRibTrfase_CS. IPR001348. ATP_PRibTrfase_HisG. IPR020621. ATP_PRibTrfase_HisG_long. IPR013115. HisG_C. [Graphical view]
PANTHER	PTHR21403. PTHR21403. 1 hit.
Pfam	PF01634. HisG. 1 hit. PF08029. HisG_C. 1 hit. [Graphical view]
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_XANCP

Accession

Primary (citable) accession number: Q8P9P3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	October 10, 2002
Last modified:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program