Reviewed, UniProtKB/Swiss-Prot P06987 (HIS7_ECOLI)

Names and origin

Protein names

Recommended name:
    Histidine biosynthesis bifunctional protein hisB
Including the following 2 domains:
    1- Recommended name:
            Histidinol-phosphatase
              EC=3.1.3.15
    2- Recommended name:
            Imidazoleglycerol-phosphate dehydratase
                Short name=IGPD
              EC=4.2.1.19

Gene names

Name:	hisB
Ordered Locus Names:	b2022, JW2004

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O. HAMAP MF_01022 L-histidinol phosphate + H2O = L-histidinol + phosphate. HAMAP MF_01022
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9. HAMAP MF_01022 Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
Subcellular location	Cytoplasm. HAMAP MF_01022
Sequence similarities	In the N-terminal section; belongs to the histidinol-phosphatase family. In the C-terminal section; belongs to the imidazoleglycerol-phosphate dehydratase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Cellular component	Cytoplasm
Molecular function	Hydrolase Lyase
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	histidinol-phosphatase activity Inferred from electronic annotation. Source: HAMAP imidazoleglycerol-phosphate dehydratase 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 – 355	355	Histidine biosynthesis bifunctional protein hisB HAMAP MF_01022		PRO_0000158206
Regions
	Region	1 – 166	166	Histidinol-phosphatase HAMAP MF_01022
	Region	167 – 355	189	Imidazoleglycerol-phosphate dehydratase HAMAP MF_01022

Sequences

	Sequence		Length	Mass (Da)
	P06987-1 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 5EC09FB68AE40A9D	FASTA	355	40,278
	10 20 30 40 50 60 MSQKYLFIDR DGTLISEPPS DFQVDRFDKL AFEPGVIPEL LKLQKAGYKL VMITNQDGLG 70 80 90 100 110 120 TQSFPQADFD GPHNLMMQIF TSQGVQFDEV LICPHLPADE CDCRKPKVKL VERYLAEQAM 130 140 150 160 170 180 DRANSYVIGD RATDIQLAEN MGITGLRYDR ETLNWPMIGE QLTRRDRYAH VVRNTKETQI 190 200 210 220 230 240 DVQVWLDREG GSKINTGVGF FDHMLDQIAT HGGFRMEINV KGDLYIDDHH TVEDTGLALG 250 260 270 280 290 300 EALKIALGDK RGICRFGFVL PMDECLARCA LDISGRPHLE YKAEFTYQRV GDLSTEMIEH 310 320 330 340 350 FFRSLSYTMG VTLHLKTKGK NDHHRVESLF KAFGRTLRQA IRVEGDTLPS SKGVL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons." Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B. J. Mol. Biol. 203:585-606(1988) [PubMed: 3062174] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Gene structure in the histidine operon of Escherichia coli. Identification and nucleotide sequence of the hisB gene." Chiariotti L., Nappo A.G., Carlomagno M.S., Bruni C.B. Mol. Gen. Genet. 202:42-47(1986) [PubMed: 3007936] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X03416 Genomic DNA. Translation: CAA27151.1. X13462 Genomic DNA. Translation: CAA31814.1. U00096 Genomic DNA. Translation: AAC75083.1. Different initiation. AP009048 Genomic DNA. Translation: BAA15853.1.
PIR	DWECHB. E64967.
RefSeq	AP_002623.1. NP_416526.4.
3D structure databases
SMR	P06987. Positions 3-165.
ModBase	Search...
2-D gel databases
SWISS-2DPAGE	P06987.
Genome annotation databases
GeneID	946552.
GenomeReviews	Gene locus JW2004 in contig AP009048_GR. Gene locus b2022 in contig U00096_GR.
KEGG	ecj:JW2004. eco:b2022.
Organism-specific databases
EchoBASE	EB0440.
EcoGene	EG10445. hisB.
CMR	Search...
Phylogenomic databases
HOGENOM	P06987.
OMA	P06987. MVSNQDG.
Enzyme and pathway databases
BioCyc	EcoCyc:IMIDPHOSPHADEHYDHISTIDPHOSPHA-MON. MetaCyc:IMIDPHOSPHADEHYDHISTIDPHOSPHA-MON.
Family and domain databases
HAMAP	MF_01022. [Tree]
InterPro	IPR006549. HAD-SF_hydro_IIIA. IPR005954. HisB_N. IPR006543. Histidinol-phos. IPR000807. Imidazole_glycer-P_deHydtase. IPR013954. PNK3P_central-region. [Graphical view]
PANTHER	PTHR23133:SF2. Imidazole-GPD. 1 hit.
Pfam	PF00475. IGPD. 1 hit. PF08645. PNK3P. 1 hit. [Graphical view]
ProDom	PD002282. IGPD. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01662. HAD-SF-IIIA. 1 hit. TIGR01261. hisB_Nterm. 1 hit. TIGR01656. Histidinol-ppas. 1 hit.
PROSITE	PS00954. IGP_DEHYDRATASE_1. 1 hit. PS00955. IGP_DEHYDRATASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS7_ECOLI

Accession

Primary (citable) accession number: P06987
Secondary accession number(s): P78077

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	June 16, 2009
This is version 83 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)