Reviewed, UniProtKB/Swiss-Prot Q02130 (HIS2_LACLA)

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:	LL1215
ORF Names:	L0072

Organism

Lactococcus lactis subsp. lactis (Streptococcus lactis) [Complete proteome] [HAMAP]

Taxonomic identifier

1360 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus

Protein attributes

Sequence length	212 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 – 212	212	Histidine biosynthesis bifunctional protein hisIE HAMAP MF_01019		PRO_0000136418
Regions
	Region	1 – 109	109	Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
	Region	110 – 212	103	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019
Experimental info
	Sequence conflict	93	1	T → A in AAB81910. Ref.1
	Sequence conflict	153	1	I → T in AAB81910. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q02130-1 [UniParc]. Last modified April 27, 2001. Version 2. Checksum: 7686EB6B923323E1	FASTA	212	24,717
	10 20 30 40 50 60 MRPDFHKQEL IPVIVQDYQT NQVLMLAYTN EVAFEKMLET GETWFWSRSR QKLWHKGEES 70 80 90 100 110 120 GHFQKIKGMR LDCDQDTLLV FVEQIGNACH TGTYSCFYDE LIPFDDSDIF SELEKQIIDR 130 140 150 160 170 180 KLHPVEKSYT NYLLGEGIDK VLKKVGEEAS EVIIASKNSD KGELLGEIDD LLYHLFVLMN 190 200 210 QQGISLEEVR QKAKERHQLE GNKKEFHTRT AD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Histidine biosynthesis genes in Lactococcus lactis subsp. lactis." Delorme C., Ehrlich S.D., Renault P. J. Bacteriol. 174:6571-6579(1992) [PubMed: 1400209] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NCDO 2118.
[2]	"The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403." Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A. Genome Res. 11:731-753(2001) [PubMed: 11337471] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: IL1403.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U92974 Genomic DNA. Translation: AAB81910.1. AE005176 Genomic DNA. Translation: AAK05313.1.
PIR	C47754. G86776.
RefSeq	NP_267371.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1114863.
GenomeReviews	Gene locus LL1215 in contig AE005176_GR.
KEGG	lla:L0072.
NMPDR	fig|272623.1.peg.1250.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q02130.
OMA	VHYWSRS.
Enzyme and pathway databases
BioCyc	LLAC272623:L0072-MON.
BRENDA	3.5.4.19. 278870. 3.6.1.31. 278870.
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_LACLA

Accession

Primary (citable) accession number: Q02130
Secondary accession number(s): Q9CG90

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	April 27, 2001
Last modified:	November 3, 2009
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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