Q9ZHE7 (HIS1_BUCAP) 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:	BUsg_092

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Schizaphis graminum)

Protein attributes

Sequence length	299 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-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00079
Cofactor	Magnesium By similarity. HAMAP-Rule MF_00079
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
Subunit structure	Equilibrium between an active dimeric form, an inactive hexameric form and higher aggregates. Interconversion between the various forms is largely reversible and is influenced by the natural substrates and inhibitors of the enzyme By similarity.
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00079.
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: 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 – 299	299	ATP phosphoribosyltransferase HAMAP-Rule MF_00079		PRO_0000151834
Experimental info
	Sequence conflict	143 – 145	3	NIV → TL Ref.1
	Sequence conflict	147 – 148	2	KS → QV Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9ZHE7 [UniParc]. Last modified August 30, 2002. Version 2. Checksum: 8E0858F490DFF1C0	FASTA	299	33,349
	10 20 30 40 50 60 MFNTNRVRIA MQKTGRLSSE SIKLLTCCGI KINLKQQKLI AFAENMPIDV MLVRDDDIPG 70 80 90 100 110 120 LVMDGVVDLG IVGENVLQEE LLHRISQNLE NSYITLRRLD FGICRLSLAI PINTPYVDIT 130 140 150 160 170 180 SLKNFRIATS YPHLLKKYLD SKNIVFKSCM LNGSVEVAPR AGLADAICDL VSTGATLEAN 190 200 210 220 230 240 GLREVQVVFR SHACLICKTG NINFAKKEVI NKLMTRIKGV IKARESKYIM LHAPVNKLEE 250 260 270 280 290 VISLLHGAEK PTILKLAGDD HRVAMHMVSS ETLFWETMEK LKSLGASSIL VLPIEKMME

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Buchnera aphidicola (Aphid endosymbiont) contains genes encoding enzymes of histidine biosynthesis." Clark M.A., Baumann L., Baumann P. Curr. Microbiol. 37:356-358(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF067228 Genomic DNA. Translation: AAC97354.1. AE013218 Genomic DNA. Translation: AAM67662.1.
RefSeq	NP_660451.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q9ZHE7.
SMR	Q9ZHE7. Positions 6-299.
ModBase	Search...
Protein-protein interaction databases
STRING	198804.BUsg092.
Proteomic databases
PRIDE	Q9ZHE7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM67662; AAM67662; BUsg_092.
GeneID	1005909.
KEGG	bas:BUsg092.
PATRIC	21246961. VBIBucAph100086_0095.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0040.
KO	K00765.
OMA	VATEFPN.
ProtClustDB	PRK00489.
Enzyme and pathway databases
BioCyc	BAPH198804:GHMG-101-MONOMER.
UniPathway	UPA00031; UER00006.
Family and domain databases
Gene3D	3.30.70.120. 1 hit.
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. 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_BUCAP

Accession

Primary (citable) accession number: Q9ZHE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 30, 2002
Last modified:	May 29, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program