P06987 (HIS7_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidine biosynthesis bifunctional protein hisB

Including the following 2 domains:

1. Histidinol-phosphatase
   EC=3.1.3.15
2. 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)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
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 Reference 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	histidinol-phosphatase activity Inferred from direct assay. Source: EcoCyc imidazoleglycerol-phosphate dehydratase 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 – 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 [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
EMBL GenBank DDBJ	X03416 Genomic DNA. Translation: CAA27151.1. X13462 Genomic DNA. Translation: CAA31814.1. U00096 Genomic DNA. Translation: AAC75083.2. AP009048 Genomic DNA. Translation: BAA15853.1.
PIR	DWECHB. E64967.
RefSeq	NP_416526.4. NC_000913.2.
3D structure databases
ProteinModelPortal	P06987.
SMR	P06987. Positions 3-346.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9901N.
IntAct	P06987. 3 interactions.
2D gel databases
SWISS-2DPAGE	P06987.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000001890; EBESCP00000001890; EBESCG00000001552. EBESCT00000001891; EBESCP00000001891; EBESCG00000001552. EBESCT00000015384; EBESCP00000014675; EBESCG00000014444.
GeneID	946552.
GenomeReviews	Gene locus JW2004 in contig AP009048_GR. Gene locus b2022 in contig U00096_GR.
KEGG	ecj:JW2004. eco:b2022.
PATRIC	32119379. VBIEscCol129921_2099.
Organism-specific databases
EchoBASE	EB0440.
EcoGene	EG10445. hisB.
Phylogenomic databases
eggNOG	COG0131.
GeneTree	EBGT00050000010149.
HOGENOM	HBG289010.
OMA	EMVPHFF.
PhylomeDB	P06987.
ProtClustDB	PRK05446.
Enzyme and pathway databases
BioCyc	EcoCyc:IMIDPHOSPHADEHYDHISTIDPHOSPHA-MONOMER. MetaCyc:IMIDPHOSPHADEHYDHISTIDPHOSPHA-MONOMER.
Gene expression databases
Genevestigator	P06987.
Family and domain databases
HAMAP	MF_01022. Bifunc_HisB. [Tree]
InterPro	IPR023214. HAD-like_dom. IPR006549. HAD-SF_hydro_IIIA. IPR020566. His_synth_bifunc_HisB. IPR005954. HisB_N. IPR006543. Histidinol-phos. IPR000807. ImidazoleglycerolP_deHydtase. IPR020565. ImidazoleglycerP_deHydtase_CS. IPR013954. PNK3P. IPR020568. Ribosomal_S5_D2-typ_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.1000. HAD-like_dom. 1 hit.
KO	K01089.
PANTHER	PTHR23133:SF2. Imidazole-GPD. 1 hit.
Pfam	PF00475. IGPD. 1 hit. PF08645. PNK3P. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit. SSF54211. Ribosomal_S5_D2-typ_fold. 2 hits.
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:	January 25, 2012
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program