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Protein

Imidazoleglycerol-phosphate dehydratase

Gene

hisB

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: L-histidine biosynthesis

This protein is involved in step 6 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase regulatory subunit (hisZ), ATP phosphoribosyltransferase (hisG)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (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. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. no protein annotated in this organism
  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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Enzyme and pathway databases

BioCyciSAUR158879:GJCB-2632-MONOMER.
UniPathwayiUPA00031; UER00011.

Names & Taxonomyi

Protein namesi
Recommended name:
Imidazoleglycerol-phosphate dehydrataseUniRule annotation (EC:4.2.1.19UniRule annotation)
Short name:
IGPDUniRule annotation
Gene namesi
Name:hisBUniRule annotation
Ordered Locus Names:SA2468
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000751 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 192192Imidazoleglycerol-phosphate dehydratasePRO_0000158167Add
BLAST

Structurei

Secondary structure

1
192
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Beta strandi13 – 219Combined sources
Beta strandi26 – 283Combined sources
Helixi32 – 4514Combined sources
Beta strandi48 – 547Combined sources
Helixi61 – 8222Combined sources
Beta strandi89 – 968Combined sources
Beta strandi99 – 1068Combined sources
Beta strandi112 – 1165Combined sources
Beta strandi122 – 1243Combined sources
Helixi131 – 14212Combined sources
Beta strandi146 – 1538Combined sources
Helixi157 – 17519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AE8X-ray2.01A/B/C/D/E/F1-192[»]
ProteinModelPortaliP64373.
SMRiP64373. Positions 1-179.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP64373.

Family & Domainsi

Sequence similaritiesi

Belongs to the imidazoleglycerol-phosphate dehydratase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000228064.
OMAiIPMDEAK.

Family and domain databases

CDDicd07914. IGPD. 1 hit.
HAMAPiMF_00076. HisB. 1 hit.
InterProiIPR000807. ImidazoleglycerolP_deHydtase.
IPR020565. ImidazoleglycerP_deHydtase_CS.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR23133:SF2. PTHR23133:SF2. 1 hit.
PfamiPF00475. IGPD. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
PROSITEiPS00954. IGP_DEHYDRATASE_1. 1 hit.
PS00955. IGP_DEHYDRATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P64373-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIYQKQRNTA ETQLNISISD DQSPSHINTG VGFLNHMLTL FTFHSGLSLN
60 70 80 90 100
IEAQGDIDVD DHHVTEDIGI VIGQLLLEMI KDKKHFVRYG TMYIPMDETL
110 120 130 140 150
ARVVVDISGR PYLSFNASLS KEKVGTFDTE LVEEFFRAVV INARLTTHID
160 170 180 190
LIRGGNTHHE IEAIFKAFSR ALGIALTATD DQRVPSSKGV IE
Length:192
Mass (Da):21,456
Last modified:October 11, 2004 - v1
Checksum:i68F9A068091BA280
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB43774.1.
PIRiD90076.
RefSeqiWP_000640266.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB43774; BAB43774; BAB43774.
PATRICi19577508. VBIStaAur116463_2672.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB43774.1.
PIRiD90076.
RefSeqiWP_000640266.1. NC_002745.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AE8X-ray2.01A/B/C/D/E/F1-192[»]
ProteinModelPortaliP64373.
SMRiP64373. Positions 1-179.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB43774; BAB43774; BAB43774.
PATRICi19577508. VBIStaAur116463_2672.

Phylogenomic databases

HOGENOMiHOG000228064.
OMAiIPMDEAK.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00011.
BioCyciSAUR158879:GJCB-2632-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP64373.

Family and domain databases

CDDicd07914. IGPD. 1 hit.
HAMAPiMF_00076. HisB. 1 hit.
InterProiIPR000807. ImidazoleglycerolP_deHydtase.
IPR020565. ImidazoleglycerP_deHydtase_CS.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR23133:SF2. PTHR23133:SF2. 1 hit.
PfamiPF00475. IGPD. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
PROSITEiPS00954. IGP_DEHYDRATASE_1. 1 hit.
PS00955. IGP_DEHYDRATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHIS7_STAAN
AccessioniPrimary (citable) accession number: P64373
Secondary accession number(s): Q99QW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: September 7, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.