Q87C28 (HIS1_XYLFT) 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:	PD_1268

Organism

Xylella fastidiosa (strain Temecula1 / ATCC 700964) [Complete proteome] [HAMAP]

Taxonomic identifier

183190 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xylella › Xylella fastidiosa

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
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_0000151876

Sequences

	Sequence		Length	Mass (Da)
	Q87C28 [UniParc]. Last modified June 16, 2003. Version 1. Checksum: 88E37467DA88AFC8	FASTA	304	33,468
	10 20 30 40 50 60 MSASTALPVR DRLRIAIQKS GRLTEPARRL LTACGLSWRQ SRDKLFCYGE SLPVDLLLVR 70 80 90 100 110 120 DDDIPGLIAQ GVCDLGIVGR NELDEQAASR RRNGLPVPYQ TLRGLHFGQC RLMLAVPEEW 130 140 150 160 170 180 EWQDISQLTG KRIATSYPAI LADWLQTHHI AAQIVELSGS VEIAPRLGTA DLICDLVSSG 190 200 210 220 230 240 ATLAAHQLKP VIQIMESQAV LAGMICQPAD ARAGLLAMLL RRIDGMVNLR DSNLLMFRAF 250 260 270 280 290 300 QEHLDALTRL LPDADPLVQL PDDGSGTLRV QTMCHGTITW QRLEELERAG AQGLMVLTVE RSLA

References

[1]

"Comparative analyses of the complete genome sequences of Pierce's disease and citrus variegated chlorosis strains of Xylella fastidiosa." Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y., Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A., Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S., Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M. , Carrer H., Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L., Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L., Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S., Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F., Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G., Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A., Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L., Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P. J. Bacteriol. 185:1018-1026(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Temecula1 / ATCC 700964.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009442 Genomic DNA. Translation: AAO29117.1.
RefSeq	NP_779468.1. NC_004556.1.
3D structure databases
ProteinModelPortal	Q87C28.
ModBase	Search...
Protein-protein interaction databases
STRING	183190.PD1268.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO29117; AAO29117; PD_1268.
GeneID	1143990.
KEGG	xft:PD1268.
PATRIC	24150637. VBIXylFas71109_1625.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0040.
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. IPR011322. N-reg_PII-like_a/b. [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_XYLFT

Accession

Primary (citable) accession number: Q87C28

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2003
Last sequence update:	June 16, 2003
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program