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Protein

Histidine biosynthesis bifunctional protein HisB

Gene

hisB

Organism
Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O.UniRule annotationSAAS annotation
L-histidinol phosphate + H2O = L-histidinol + phosphate.UniRule annotationSAAS annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotationSAAS annotation
  • Zn2+UniRule annotation

Pathwayi: L-histidine biosynthesis

This protein is involved in step 6 and 8 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotationSAAS annotation
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (hisI), Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Histidine biosynthesis bifunctional protein HisB (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. Histidine biosynthesis bifunctional protein HisB (hisB)
  9. Histidinol dehydrogenase (hisD)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei10NucleophileUniRule annotation1
Metal bindingi10MagnesiumUniRule annotation1
Active sitei12Proton donorUniRule annotation1
Metal bindingi12Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi94ZincUniRule annotation1
Metal bindingi96Zinc; via pros nitrogenUniRule annotation1
Metal bindingi102ZincUniRule annotation1
Metal bindingi104ZincUniRule annotation1
Metal bindingi131MagnesiumUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolaseUniRule annotationSAAS annotationImported, LyaseUniRule annotationSAAS annotationImported
Biological processAmino-acid biosynthesis, Histidine biosynthesisUniRule annotationSAAS annotation
LigandMagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, ZincUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00031; UER00011.
UPA00031; UER00013.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine biosynthesis bifunctional protein HisBUniRule annotation
Including the following 2 domains:
Histidinol-phosphataseUniRule annotation (EC:3.1.3.15UniRule annotation)
Imidazoleglycerol-phosphate dehydrataseUniRule annotation (EC:4.2.1.19UniRule annotation)
Short name:
IGPDUniRule annotation
Gene namesi
Name:hisBUniRule annotation
Ordered Locus Names:MADE_1012310Imported
OrganismiAlteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype)Imported
Taxonomic identifieri1774373 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas
Proteomesi
  • UP000001870 Componenti: Chromosome

Subcellular locationi

F2G6W4:
  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Structurei

3D structure databases

ProteinModelPortaliF2G6W4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 167Histidinol-phosphataseUniRule annotationAdd BLAST167
Regioni168 – 356Imidazoleglycerol-phosphate dehydrataseUniRule annotationAdd BLAST189

Sequence similaritiesi

In the C-terminal section; belongs to the imidazoleglycerol-phosphate dehydratase family.UniRule annotationSAAS annotation
In the N-terminal section; belongs to the histidinol-phosphatase family.UniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiENOG4105ECC. Bacteria.
COG0131. LUCA.
COG0241. LUCA.
KOiK01089.

Family and domain databases

CDDicd07914. IGPD. 1 hit.
Gene3Di3.40.50.1000. 1 hit.
HAMAPiMF_01022. Bifunc_HisB. 1 hit.
MF_00076. HisB. 1 hit.
InterProiView protein in InterPro
IPR036412. HAD-like_sf.
IPR006549. HAD-SF_hydro_IIIA.
IPR023214. HAD_sf.
IPR020566. His_synth_bifunc_HisB.
IPR005954. HisB_N.
IPR006543. Histidinol-phos.
IPR000807. ImidazoleglycerolP_deHydtase.
IPR020565. ImidazoleglycerP_deHydtase_CS.
IPR020568. Ribosomal_S5_D2-typ_fold.
PANTHERiPTHR23133. PTHR23133. 1 hit.
PfamiView protein in Pfam
PF00475. IGPD. 1 hit.
SUPFAMiSSF54211. SSF54211. 2 hits.
SSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01261. hisB_Nterm. 1 hit.
TIGR01656. Histidinol-ppas. 1 hit.
PROSITEiView protein in PROSITE
PS00954. IGP_DEHYDRATASE_1. 1 hit.

Sequencei

Sequence statusi: Complete.

F2G6W4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQQAILFID RDGTLVEEPP IDKQLDSLEK LVFEPNVIPV LLKLKASDFK
60 70 80 90 100
LVMVSNQDGL GTDSFPQEDF DKPHNAMMAI FESQGVTFDD VLICPHFDED
110 120 130 140 150
NCTCRKPKLG LVQEYLQKGK VDFTRSFVIG DRITDVQLAE NMGIRSFQYN
160 170 180 190 200
RESLNWNDIQ KSLLASSRIA EVVRTTSETD IKVRVDLDSQ AKSTIQTGMG
210 220 230 240 250
FFDHMLDQIA THGGFELNLT TNGDLHIDDH HSVEDTALAL GEALKKALGD
260 270 280 290 300
KRGIGRFGFA LPMDECRAEC IMDISNRPHL KFDAEFSRDQ VGEMATEMVP
310 320 330 340 350
HFFYSLAQSM GLSLHLSTSE GNAHHQVESL FKVFGRALRQ AITRQGDALP

SSKGAL
Length:356
Mass (Da):39,757
Last modified:May 31, 2011 - v1
Checksum:i415B4859B1A3BEA2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001103 Genomic DNA. Translation: AEA98598.1.
RefSeqiWP_012518916.1. NC_011138.3.

Genome annotation databases

EnsemblBacteriaiAEA98598; AEA98598; MADE_1012310.
KEGGiamc:MADE_1012310.

Similar proteinsi

Entry informationi

Entry nameiF2G6W4_ALTMD
AccessioniPrimary (citable) accession number: F2G6W4
Entry historyiIntegrated into UniProtKB/TrEMBL: May 31, 2011
Last sequence update: May 31, 2011
Last modified: October 25, 2017
This is version 56 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported, Multifunctional enzymeUniRule annotationSAAS annotation