Reviewed, UniProtKB/Swiss-Prot Q8PLG5 (HIS2_XANAC)

Names and origin

Protein names

Recommended name:
    Histidine biosynthesis bifunctional protein hisIE
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosyl-AMP cyclohydrolase
                Short name=PRA-CH
              EC=3.5.4.19
    2- Recommended name:
            Phosphoribosyl-ATP pyrophosphatase
                Short name=PRA-PH
              EC=3.6.1.31

Gene names

Name:	hisI
Synonyms:	hisIE
Ordered Locus Names:	XAC1835

Organism

Xanthomonas axonopodis pv. citri (Citrus canker) [Complete proteome] [HAMAP]

Taxonomic identifier

92829 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

Protein attributes

Sequence length	206 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	1-(5-phosphoribosyl)-ATP + H2O = 1-(5-phosphoribosyl)-AMP + diphosphate. HAMAP MF_01019 1-(5-phosphoribosyl)-AMP + H2O = 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide. HAMAP MF_01019
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. HAMAP MF_01019 Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	In the N-terminal section; belongs to the PRA-CH family. In the C-terminal section; belongs to the PRA-PH family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome Multifunctional enzyme
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 phosphoribosyl-AMP cyclohydrolase activity Inferred from electronic annotation. Source: HAMAP phosphoribosyl-ATP diphosphatase activity 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 – 206	206	Histidine biosynthesis bifunctional protein hisIE HAMAP MF_01019		PRO_0000136450
Regions
	Region	1 – 117	117	Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
	Region	118 – 206	89	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

	Sequence		Length	Mass (Da)
	Q8PLG5-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 1B04984CEEFBD377	FASTA	206	22,262
	10 20 30 40 50 60 MGSNEVATGD PLATLDWNKG EGLLPVIVQD ADNLRVLMLG YMNAQALAVT QQRGEVTFFS 70 80 90 100 110 120 RSKQRLWTKG ESSGNVLRVV SIQTDCDADT LLVQARPHGP TCHLGRTSCF PSAPGQFLGS 130 140 150 160 170 180 LDALVAERER ERPHGSYTTK LFEQGIRRIA QKVGEEGVET ALAGVVQDDD ALLGESADLL 190 200 YHLIVLLRAR GLGLGDAAAL LESRHQ

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed: 12024217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 306.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE011816 Genomic DNA. Translation: AAM36697.1.
RefSeq	NP_642161.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1155906.
GenomeReviews	Gene locus XAC1835 in contig AE008923_GR.
KEGG	xac:XAC1835.
NMPDR	fig|190486.1.peg.1805.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8PLG5.
OMA	Q8PLG5. VHYWSRS.
Enzyme and pathway databases
BioCyc	XAXO190486:XAC1835-MON.
BRENDA	3.5.4.19. 289771. 3.6.1.31. 289771.
Family and domain databases
HAMAP	MF_01019. [Tree]
InterPro	IPR002496. PRA_CycHdrlase. IPR008179. PRib-ATP_pyrophosphohydrolase. [Graphical view]
Pfam	PF01502. PRA-CH. 1 hit. PF01503. PRA-PH. 1 hit. [Graphical view]
ProDom	PD002610. PRA_cyclohydro. 1 hit. PD002611. Pra_PH/CH. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03188. histidine_hisI. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HIS2_XANAC

Accession

Primary (citable) accession number: Q8PLG5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	October 1, 2002
Last modified:	June 16, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)