Reviewed, UniProtKB/Swiss-Prot Q9PM76 (HIS7_CAMJE)

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:	Cj1599

Organism

Campylobacter jejuni [Complete proteome] [HAMAP]

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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 By similarity.
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 – 352	352	Histidine biosynthesis bifunctional protein hisB HAMAP MF_01022		PRO_0000158204
Regions
	Region	1 – 164	164	Histidinol-phosphatase HAMAP MF_01022
	Region	165 – 352	188	Imidazoleglycerol-phosphate dehydratase HAMAP MF_01022

Sequences

	Sequence		Length	Mass (Da)
	Q9PM76-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 522FDD31CC01A656	FASTA	352	39,580
	10 20 30 40 50 60 MSQKILFIDR DGTLIEEPKS DFQIDTLEKL RFEKDAIPTL LKLKKFGFKF VMVSNQDGLG 70 80 90 100 110 120 TPSFPKENFE IAHEKMLDIL KSCGIEFQDI FICPHFENEN CACRKPKTAM LEEYIKHELY 130 140 150 160 170 180 DKEQSFVIGD RESDMILASN LGVRGLKYGE LSWKEIENEI LSSFRSASYQ RTTKETDIKV 190 200 210 220 230 240 KVCLNGGKVS IKTGIDFFDH MLEQIAVHGG IGLEISCKGD LEIDEHHSVE DVALALGACI 250 260 270 280 290 300 KKALGDKIGI ARYGFALPMD ECLASCAMDF CNRPHLVYKA KFKKSHLGAL STEMIEHFFY 310 320 330 340 350 SLSYAMGVSL HLKVKGKNDH HKAEGLFKAF AKALKMAVKI ESENLASSKG VI

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL111168 Genomic DNA. Translation: CAL35696.1.
PIR	E81255.
RefSeq	YP_002344968.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9PM76. 30 interactions.
Genome annotation databases
GeneID	905869.
GenomeReviews	Gene locus Cj1599 in contig AL111168_GR.
KEGG	cje:Cj1599.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	Q9PM76. MVSNQDG.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ1599-MON.
BRENDA	3.1.3.15. 255835. 4.2.1.19. 255835.
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_CAMJE

Accession

Primary (citable) accession number: Q9PM76
Secondary accession number(s): Q0P829

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 24, 2002
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 50 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)