Q01ZU0 (HIS1_SOLUE) 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:	Acid_3856

Organism

Solibacter usitatus (strain Ellin6076) [Complete proteome] [HAMAP]

Taxonomic identifier

234267 [NCBI]

Taxonomic lineage

Bacteria › Acidobacteria › Solibacteres › Solibacterales › Solibacteraceae › Candidatus Solibacter

Protein attributes

Sequence length	289 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 MF_00079
Catalytic activity	1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_00079
Cofactor	Magnesium By similarity. HAMAP MF_00079
Enzyme regulation	Feedback inhibited by histidine By similarity. HAMAP MF_00079
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. HAMAP MF_00079
Subcellular location	Cytoplasm By similarity HAMAP 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-KW
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 – 289	289	ATP phosphoribosyltransferase HAMAP MF_00079		PRO_1000118259

Sequences

	Sequence		Length	Mass (Da)
	Q01ZU0 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 683CDA61BFD3D6EF	FASTA	289	31,952
	10 20 30 40 50 60 MLLKLGIPKG SLENATIDLF RRAGFQITTS SRSYFPGIDD PEIECMLIRA QEMARYVEDG 70 80 90 100 110 120 ILDSGLTGRD WIEENEAAIV PVADLIYAKQ SFGKVRWVLA VPEASSFRTV HDLEGKIIAT 130 140 150 160 170 180 ELVATTKRYM AKHGVKAKVE FSWGATEVKP PVLADAIVEV TETGSSLRAN KLKIIDTVLE 190 200 210 220 230 240 SNTQLIANKA SWEDPEKRRK LEDIRMLLQG AINALGKVGL MLNVHKDNLK AVLGVLPALK 250 260 270 280 RPTISHLSDD EWLAVNTILD ESTVRDIIPR LKQAGGEGIV EYPLNKIVL

References

[1]

"Three genomes from the phylum Acidobacteria provide insight into the lifestyles of these microorganisms in soils." Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., Davidsen T.M. , DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R. Appl. Environ. Microbiol. 75:2046-2056(2009) [PubMed: 19201974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ellin6076.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000473 Genomic DNA. Translation: ABJ84825.1.
RefSeq	YP_825110.1. NC_008536.1.
3D structure databases
ProteinModelPortal	Q01ZU0.
ModBase	Search...
Protein-protein interaction databases
STRING	Q01ZU0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4426656.
GenomeReviews	Gene locus Acid_3856 in contig CP000473_GR.
KEGG	sus:Acid_3856.
NMPDR	fig|234267.9.peg.3665.
PATRIC	32010136. VBICanSol30224_4034.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0040.
HOGENOM	HBG391868.
OMA	IMLHAPS.
PhylomeDB	Q01ZU0.
ProtClustDB	PRK00489.
Family and domain databases
HAMAP	MF_00079. HisG_Long. [Tree]
InterPro	IPR013820. ATP_PRibTrfase_cat. 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]
Gene3D	G3DSA:3.30.70.120. PII_glnB. 1 hit.
KO	K00765.
PANTHER	PTHR21403. ATP_phspho_trans. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS1_SOLUE

Accession

Primary (citable) accession number: Q01ZU0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program