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Reviewed, UniProtKB/Swiss-Prot Q1LT69 (HIS7_BAUCH)

Last modified June 16, 2009. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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: BCI_0402
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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 processAmino-acid biosynthesis
Histidine biosynthesis
   Cellular componentCytoplasm
   Molecular functionHydrolase
Lyase
   Technical termComplete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological processhistidine biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhistidinol-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Histidine biosynthesis bifunctional protein hisB HAMAP MF_01022
PRO_1000063441

Regions

Region1 – 166166Histidinol-phosphatase HAMAP MF_01022
Region167 – 356190Imidazoleglycerol-phosphate dehydratase HAMAP MF_01022

Sequences

Sequence LengthMass (Da)Tools
Q1LT69-1 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 3D2AF3DAD6D75C53

FASTA35640,624
        10         20         30         40         50         60 
MSKKVLFIDR DGTLINEPLD NFQIDRIEKL VLEPYVINAL LILQQANFQL VMVSNQDGLG 

        70         80         90        100        110        120 
TSSFPQEDFD RPHNLMMQIF KSQNIFFDQV LICPHLAKDK CHCRKPGIAL VAPWLVGNKI 

       130        140        150        160        170        180 
DRTKSYVIGD RETDIKLAYN MGINSLRYNR NTMNWQAICN YLTSLNRYAH VKRITKETSI 

       190        200        210        220        230        240 
NVEVWLDREA PSKINTGINF FDHMLEQIAT HSGLCMTIEV KGDLYIDDHH TIEDTAIALG 

       250        260        270        280        290        300 
TALKQGLGDK HGINRFGFLL PMDECLARCV IDLSGRPFLE YTAEYSYQKV GDMSTEMVEH 

       310        320        330        340        350 
FFRSLSYAMA CTLYLKTEGK NDHHRVESLF KVFGRALRQA ICVESNVLPS SKGVLS 

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References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000238 Genomic DNA. Translation: ABF13797.1.
RefSeqYP_588845.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4056379.
GenomeReviewsGene locus BCI_0402 in contig CP000238_GR.
KEGGbci:BCI_0402.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1LT69.
OMAQ1LT69. MVSNQDG.

Family and domain databases

HAMAPMF_01022.
[Tree]
InterProIPR006549. HAD-SF_hydro_IIIA.
IPR005954. HisB_N.
IPR006543. Histidinol-phos.
IPR000807. Imidazole_glycer-P_deHydtase.
[Graphical view]
PANTHERPTHR23133:SF2. Imidazole-GPD. 1 hit.
PfamPF00475. IGPD. 1 hit.
[Graphical view]
ProDomPD002282. IGPD. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01261. hisB_Nterm. 1 hit.
TIGR01656. Histidinol-ppas. 1 hit.
PROSITEPS00954. IGP_DEHYDRATASE_1. 1 hit.
PS00955. IGP_DEHYDRATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHIS7_BAUCH
AccessionPrimary (citable) accession number: Q1LT69
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 30, 2006
Last modified: June 16, 2009
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents