P37793 (HIS2_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidine biosynthesis bifunctional protein HisIE

Including the following 2 domains:

1. Phosphoribosyl-AMP cyclohydrolase
   Short name=PRA-CH
   EC=3.5.4.19
2. Phosphoribosyl-ATP pyrophosphatase
   Short name=PRA-PH
   EC=3.6.1.31

Gene names

Name:	hisI
Synonyms:	hisIE
Ordered Locus Names:	SF2088, S2209

Organism

Shigella flexneri [Complete proteome] [HAMAP]

Taxonomic identifier

623 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	203 AA.
Sequence status	Complete.
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 HAMAP MF_01019.
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: UniProtKB-KW
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: EC phosphoribosyl-ATP diphosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 203	203	Histidine biosynthesis bifunctional protein HisIE HAMAP MF_01019		PRO_0000136429
Regions
	Region	1 – 114	114	Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
	Region	115 – 203	89	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

	Sequence		Length	Mass (Da)
	P37793 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 51EC7BDA1D0BAEC0	FASTA	203	22,882
	10 20 30 40 50 60 MLTEQQRREL DWEKTDGLMP VIVQHAVSGE VLMLGYMNPE ALDKTIESGK VTFFSRTKQR 70 80 90 100 110 120 LWIKGETSGN FLNVVSIAPD CDNDTLLVLA NPIGPTCHKG TSSCFGNTAH QWLFLYQLEQ 130 140 150 160 170 180 LLAERKYADP ETSYTAKLYA SGTKRIAQKV GEEGVETALA ATVHDRFELT NEASDLMYHL 190 200 LVLLQDQDLD LTTVIENLHK RHQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the rfc region of Shigella flexneri." Morona R., Mavris M., Fallarino A., Manning P.A. J. Bacteriol. 176:733-747(1994) [PubMed: 7507920] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PE577 / Serotype 2a.
[2]	"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J. Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a.
[3]	"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X71970 Genomic DNA. Translation: CAA50784.1. AE005674 Genomic DNA. Translation: AAN43628.1. AE014073 Genomic DNA. Translation: AAP17456.1.
RefSeq	NP_707921.1. NC_004337.2. NP_837647.1. NC_004741.1.
3D structure databases
ProteinModelPortal	P37793.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000088202; EBESCP00000085024; EBESCG00000087247. EBESCT00000089458; EBESCP00000086094; EBESCG00000088502.
GeneID	1025295. 1078510.
GenomeReviews	Gene locus SF2088 in contig AE005674_GR. Gene locus S2209 in contig AE014073_GR.
KEGG	sfl:SF2088. sfx:S2209.
PATRIC	18705937. VBIShiFle31049_2447.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000011321.
HOGENOM	HBG294308.
OMA	VMACKDD.
ProtClustDB	PRK02759.
Enzyme and pathway databases
BioCyc	SFLE198214:AAN43628.1-MONOMER.
Family and domain databases
HAMAP	MF_01019. HisIE. [Tree]
InterPro	IPR023019. His_synth_HisIE. IPR008179. PRib-ATP_PPHydrolase. IPR021130. PRib-ATP_PPHydrolase-like. IPR002496. PRib_AMP_CycHydrolase. [Graphical view]
KO	K11755.
Pfam	PF01502. PRA-CH. 1 hit. PF01503. PRA-PH. 1 hit. [Graphical view]
ProDom	PD002610. PRA_CycHdrlase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03188. Histidine_hisI. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HIS2_SHIFL

Accession

Primary (citable) accession number: P37793

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	January 25, 2012
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program