A1KKG4 (HIS1_MYCBP) 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:	BCG_2138c

Organism

Mycobacterium bovis (strain BCG / Pasteur 1173P2) [Complete proteome] [HAMAP]

Taxonomic identifier

410289 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium bovis › Mycobacterium bovis BCG

Protein attributes

Sequence length	284 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
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.
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 – 284	284	ATP phosphoribosyltransferase HAMAP-Rule MF_00079		PRO_1000004475

Sequences

	Sequence		Length	Mass (Da)
	A1KKG4 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: C248C57399302B2A	FASTA	284	30,481
	10 20 30 40 50 60 MLRVAVPNKG ALSEPATEIL AEAGYRRRTD SKDLTVIDPV NNVEFFFLRP KDIAIYVGSG 70 80 90 100 110 120 ELDFGITGRD LVCDSGAQVR ERLALGFGSS SFRYAAPAGR NWTTADLAGM RIATAYPNLV 130 140 150 160 170 180 RKDLATKGIE ATVIRLDGAV EISVQLGVAD AIADVVGSGR TLSQHDLVAF GEPLCDSEAV 190 200 210 220 230 240 LIERAGTDGQ DQTEARDQLV ARVQGVVFGQ QYLMLDYDCP RSALKKATAI TPGLESPTIA 250 260 270 280 PLADPDWVAI RALVPRRDVN GIMDELAAIG AKAILASDIR FCRF

References

[1]

"Genome plasticity of BCG and impact on vaccine efficacy." Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T. Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BCG / Pasteur 1173P2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM408590 Genomic DNA. Translation: CAL72126.1.
RefSeq	YP_978227.1. NC_008769.1.
3D structure databases
ProteinModelPortal	A1KKG4.
SMR	A1KKG4. Positions 1-284.
ModBase	Search...
Protein-protein interaction databases
STRING	410289.BCG_2138c.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAL72126; CAL72126; BCG_2138c.
GeneID	4699083.
KEGG	mbb:BCG_2138c.
PATRIC	18015154. VBIMycBov80988_2338.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0040.
HOGENOM	HOG000223250.
KO	K00765.
OMA	VATEFPN.
ProtClustDB	PRK00489.
Enzyme and pathway databases
BioCyc	MBOV410289:GJW7-2164-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...
Other
BindingDB	A1KKG4.

Entry information

Entry name

HIS1_MYCBP

Accession

Primary (citable) accession number: A1KKG4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 6, 2007
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program