C0ZZV7 (HIS1_RHOE4) 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:	RER_31840

Organism

Rhodococcus erythropolis (strain PR4 / NBRC 100887) [Complete proteome] [HAMAP]

Taxonomic identifier

234621 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus › Rhodococcus erythropolis

Protein attributes

Sequence length	283 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
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 – 283	283	ATP phosphoribosyltransferase HAMAP-Rule MF_00079		PRO_1000202536

Sequences

	Sequence		Length	Mass (Da)
	C0ZZV7 [UniParc]. Last modified May 26, 2009. Version 1. Checksum: E27600EB8BA96DB4	FASTA	283	30,477
	10 20 30 40 50 60 MLRVAVPNKG SLSESAAEIL SEAGYRRRTD SRDLTVLDPA NQVEFFFLRP KDIAIYVGSG 70 80 90 100 110 120 ELDLGITGRD LAGDSGAPVS ERLSLGFGRS SFRYAAPAGK DWAVEDLSGL RIATSYPNLV 130 140 150 160 170 180 RKDLTDRGLD ATVIRLDGAV EISIQLGVAD AIADVVGSGR TLRQHNLVAF GESLCDSEGV 190 200 210 220 230 240 LIERTGAPQD DPARNQLIER VRGIVFAQQN LMIDYDCPRT ILDDAIKMTP GMESPTLSPL 250 260 270 280 ADPDWVAVRA MVPIKGHNQV MDALAELGAK AILASNIRSV RAF

References

[1]

"Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4." Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PR4 / NBRC 100887.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP008957 Genomic DNA. Translation: BAH33892.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	234621.RER_31840.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAH33892; BAH33892; RER_31840.
KEGG	rer:RER_31840.
PATRIC	23192810. VBIRhoEry66701_3690.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0040.
HOGENOM	HOG000223250.
KO	K00765.
OMA	EGKHIAT.
ProtClustDB	PRK00489.
Enzyme and pathway databases
BioCyc	RERY234621:GHDE-3218-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_RHOE4

Accession

Primary (citable) accession number: C0ZZV7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	May 26, 2009
Last modified:	May 29, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program