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Protein

Imidazoleglycerol-phosphate dehydratase

Gene

hisB

Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Status
Reviewed-Annotation score: Annotation score: 2 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 annotation

Pathwayi

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

BioCyciCVIO243365:GHUD-624-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:CV_0614
OrganismiChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Taxonomic identifieri243365 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium
ProteomesiUP000001424 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 – 197197Imidazoleglycerol-phosphate dehydratasePRO_0000158123Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243365.CV_0614.

Structurei

3D structure databases

ProteinModelPortaliQ7P0F3.
SMRiQ7P0F3. Positions 2-183.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the imidazoleglycerol-phosphate dehydratase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0131.
HOGENOMiHOG000228064.
KOiK01693.
OMAiHHIVEAC.
OrthoDBiEOG60PHGP.

Family and domain databases

HAMAPiMF_00076. HisB.
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.

Q7P0F3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTATVTRNT LETQITVSLN LDGTGVGRFE TGVPFLDHMM DQIARHGLID
60 70 80 90 100
LDVKAVGDLH IDAHHTVEDI GITLGQAFAK AIGDKKGIRR YGHAYVPLDE
110 120 130 140 150
ALSRVVIDLS GRPGLVYNVD YTRACIGQFD VDLFSEFFHG FVNHSMVTLH
160 170 180 190
IDNLRGHNSH HQAETIFKAF GRALRMACEH DERMAGITPS TKGTLSV
Length:197
Mass (Da):21,752
Last modified:December 15, 2003 - v1
Checksum:iAE696FF868135312
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016825 Genomic DNA. Translation: AAQ58290.1.
RefSeqiNP_900284.1. NC_005085.1.
WP_011134169.1. NC_005085.1.

Genome annotation databases

EnsemblBacteriaiAAQ58290; AAQ58290; CV_0614.
KEGGicvi:CV_0614.
PATRICi21436024. VBIChrVio67196_0613.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016825 Genomic DNA. Translation: AAQ58290.1.
RefSeqiNP_900284.1. NC_005085.1.
WP_011134169.1. NC_005085.1.

3D structure databases

ProteinModelPortaliQ7P0F3.
SMRiQ7P0F3. Positions 2-183.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243365.CV_0614.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAQ58290; AAQ58290; CV_0614.
KEGGicvi:CV_0614.
PATRICi21436024. VBIChrVio67196_0613.

Phylogenomic databases

eggNOGiCOG0131.
HOGENOMiHOG000228064.
KOiK01693.
OMAiHHIVEAC.
OrthoDBiEOG60PHGP.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00011.
BioCyciCVIO243365:GHUD-624-MONOMER.

Family and domain databases

HAMAPiMF_00076. HisB.
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...

Publicationsi

  1. "The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
    Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A.
    , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
    Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Entry informationi

Entry nameiHIS7_CHRVO
AccessioniPrimary (citable) accession number: Q7P0F3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: December 15, 2003
Last modified: May 27, 2015
This is version 84 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.