Q87QL2 (HIS1_VIBPA) 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:	VP1137

Organism

Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]

Taxonomic identifier

223926 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › Vibrio harveyi group › Vibrio parahaemolyticus

Protein attributes

Sequence length	298 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.
Sequence caution	The sequence BAC59400.1 differs from that shown. Reason: Erroneous initiation.

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 – 298	298	ATP phosphoribosyltransferase HAMAP-Rule MF_00079		PRO_0000151870

Sequences

	Sequence		Length	Mass (Da)
	Q87QL2 [UniParc]. Last modified May 23, 2003. Version 1. Checksum: 1DC3A1620CA4F108	FASTA	298	32,845
	10 20 30 40 50 60 MQTQRLRIAI QKKGRLSKES QALLKQCGVK FNVMGERLVV HSENMPIDLL LVRDDDIPGL 70 80 90 100 110 120 IMDGVVDLGF IGENELEEVR LDRKALGEPC EFVQLRRLDF GGCRLSIAID KDEEYNGPQD 130 140 150 160 170 180 LAGKRIATTY PQLLKAYMDE AGVPFSTCML TGSVEVAPRA GLADAIADLV STGATLEANG 190 200 210 220 230 240 LKEAEVIFRS KATLIQRIGE FDADKAELIN KLLTRMQGVQ QAKESKYIML HAPAGKLEQI 250 260 270 280 290 KALLPGAEDP TVLPLSADKQ KVAVHLVSTE NLFWETMEQL KELGASSILV LPIEKMME

References

[1]

"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae." Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T. Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RIMD 2210633.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000031 Genomic DNA. Translation: BAC59400.1. Different initiation.
RefSeq	NP_797516.1. NC_004603.1.
3D structure databases
ProteinModelPortal	Q87QL2.
SMR	Q87QL2. Positions 5-298.
ModBase	Search...
Protein-protein interaction databases
STRING	223926.VP1137.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAC59400; BAC59400; BAC59400.
GeneID	1188642.
KEGG	vpa:VP1137.
PATRIC	20140484. VBIVibPar50997_1079.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0040.
HOGENOM	HOG000223247.
KO	K00765.
OMA	VATEFPN.
ProtClustDB	PRK00489.
Enzyme and pathway databases
BioCyc	VPAR223926:GHK4-1186-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_VIBPA

Accession

Primary (citable) accession number: Q87QL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 23, 2003
Last sequence update:	May 23, 2003
Last modified:	May 29, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program