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Q2NTX3 (HIS7_SODGM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:SG1127
OrganismSodalis glossinidius (strain morsitans) [Complete proteome] [HAMAP]
Taxonomic identifier343509 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSodalis

Protein attributes

Sequence length355 AA.
Sequence statusComplete.
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 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 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: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhistidinol-phosphatase activity

Inferred from electronic annotation. Source: EC

imidazoleglycerol-phosphate dehydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 355355Histidine biosynthesis bifunctional protein hisB HAMAP MF_01022
PRO_1000063449

Regions

Region1 – 166166Histidinol-phosphatase HAMAP MF_01022
Region167 – 355189Imidazoleglycerol-phosphate dehydratase HAMAP MF_01022

Sequences

Sequence LengthMass (Da)Tools
Q2NTX3 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 0BDC33A77F10CC7E

FASTA35539,469
        10         20         30         40         50         60 
MNQKVLFIDR DGTLINEPPA DFQVDRMDKL ALEPGVIPVL LALQKAGFRL VMITNQDGLG 

        70         80         90        100        110        120 
TTSFPQADFD GPHDLMMAIF TSQGIVFDEV LICPHLPTDG CACRKPQTGI VTPWLKEHAL 

       130        140        150        160        170        180 
DSAHSYVIGD RETDMALAAN MGITGLRYQR ASLNWPAIGE QLTRSDRHAR VNRVTRETAI 

       190        200        210        220        230        240 
DVEVWLDREG DSRINTGIGF FDHMLDQIAT HGGLRINIAV KGDLHIDDHH TVEDTALALG 

       250        260        270        280        290        300 
EALNKALGDK RGIGRFGFVL PMDECLARCA LDISGRPHLE YKAKYSFQRV GDLSTEMVEH 

       310        320        330        340        350 
FFRSLSYAMA CTLHLRTKGK NDHHRVESLF KAFGRTLRQA IRVEGDTLPS SKGVL 

« Hide

References

[1]"Massive genome erosion and functional adaptations provide insights into the symbiotic lifestyle of Sodalis glossinidius in the tsetse host."
Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M., Aksoy S.
Genome Res. 16:149-156(2006) [PubMed: 16365377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: morsitans.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008232 Genomic DNA. Translation: BAE74402.1.
RefSeqYP_454807.1. NC_007712.1.

3D structure databases

ProteinModelPortalQ2NTX3.
SMRQ2NTX3. Positions 3-164, 167-344.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2NTX3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3867555.
GenomeReviewsGene locus SG1127 in contig AP008232_GR.
KEGGsgl:SG1127.
NMPDRfig|343509.6.peg.2310.
PATRIC23650510. VBISodGlo61428_2564.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0131.
HOGENOMHBG289010.
OMAEMVPHFF.
PhylomeDBQ2NTX3.
ProtClustDBPRK05446.

Enzyme and pathway databases

BioCycSGLO343509:SG1127-MONOMER.

Family and domain databases

HAMAPMF_01022. Bifunc_HisB.
[Tree]
InterProIPR023214. 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]
Gene3DG3DSA:3.40.50.1000. HAD-like_dom. 1 hit.
KOK01089.
PANTHERPTHR23133:SF2. Imidazole-GPD. 1 hit.
PfamPF00475. IGPD. 1 hit.
PF08645. PNK3P. 1 hit.
[Graphical view]
SUPFAMSSF56784. HAD-like_dom. 1 hit.
SSF54211. Ribosomal_S5_D2-typ_fold. 2 hits.
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_SODGM
AccessionPrimary (citable) accession number: Q2NTX3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 7, 2006
Last modified: January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families