Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8G0L3

- HIS3_BRUSU

UniProt

Q8G0L3 - HIS3_BRUSU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Phosphoribosyl-AMP cyclohydrolase

Gene

hisI

Organism
Brucella suis biovar 1 (strain 1330)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.UniRule annotation

Catalytic activityi

1-(5-phospho-beta-D-ribosyl)-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotationNote: Binds 1 Mg(2+) ion per subunit.UniRule annotation
  • Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi91 – 911MagnesiumUniRule annotation
Metal bindingi92 – 921Zinc; shared with dimeric partnerUniRule annotation
Metal bindingi93 – 931MagnesiumUniRule annotation
Metal bindingi95 – 951MagnesiumUniRule annotation
Metal bindingi110 – 1101Zinc; shared with dimeric partnerUniRule annotation
Metal bindingi117 – 1171Zinc; shared with dimeric partnerUniRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphoribosyl-AMP cyclohydrolase activity Source: UniProtKB-EC

GO - Biological processi

  1. histidine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00031; UER00008.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosyl-AMP cyclohydrolaseUniRule annotation (EC:3.5.4.19UniRule annotation)
Short name:
PRA-CHUniRule annotation
Gene namesi
Name:hisIUniRule annotation
Ordered Locus Names:BR1076, BS1330_I1072
OrganismiBrucella suis biovar 1 (strain 1330)
Taxonomic identifieri204722 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000000824: Chromosome I, UP000007104: Chromosome I

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 139139Phosphoribosyl-AMP cyclohydrolasePRO_0000136467Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi204722.BR1076.

Structurei

3D structure databases

ProteinModelPortaliQ8G0L3.
SMRiQ8G0L3. Positions 18-124.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PRA-CH family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0139.
HOGENOMiHOG000277504.
KOiK01496.
OrthoDBiEOG6PGKB6.

Family and domain databases

HAMAPiMF_01021. HisI.
InterProiIPR026660. PRA-CH.
IPR002496. PRib_AMP_CycHydrolase_dom.
[Graphical view]
PfamiPF01502. PRA-CH. 1 hit.
[Graphical view]
ProDomiPD002610. PRA_CycHdrlase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

Q8G0L3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSIFPAQPSD KKAVEEGAAF MPRFDASGLI TAIVTDARDG ELLMVAHMNE
60 70 80 90 100
EALRLTLETG IAHYWSRSRK TLWKKGETSG NLQSVVELRT DCDQDALWLK
110 120 130
VHVAGDGPTC HTGRRSCFYR QVVSSGGKVA LTMVSDHDQ
Length:139
Mass (Da):15,308
Last modified:November 7, 2003 - v2
Checksum:iA150156774661556
GO

Sequence cautioni

The sequence AAN29996.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014291 Genomic DNA. Translation: AAN29996.1. Different initiation.
CP002997 Genomic DNA. Translation: AEM18414.1.
RefSeqiNP_698081.2. NC_004310.3.
YP_005615906.1. NC_017251.1.

Genome annotation databases

EnsemblBacteriaiAAN29996; AAN29996; BR1076.
AEM18414; AEM18414; BS1330_I1072.
GeneIDi1166750.
12138103.
KEGGibms:BR1076.
bsi:BS1330_I1072.
PATRICi17790470. VBIBruSui107850_1090.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014291 Genomic DNA. Translation: AAN29996.1 . Different initiation.
CP002997 Genomic DNA. Translation: AEM18414.1 .
RefSeqi NP_698081.2. NC_004310.3.
YP_005615906.1. NC_017251.1.

3D structure databases

ProteinModelPortali Q8G0L3.
SMRi Q8G0L3. Positions 18-124.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 204722.BR1076.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN29996 ; AAN29996 ; BR1076 .
AEM18414 ; AEM18414 ; BS1330_I1072 .
GeneIDi 1166750.
12138103.
KEGGi bms:BR1076.
bsi:BS1330_I1072.
PATRICi 17790470. VBIBruSui107850_1090.

Phylogenomic databases

eggNOGi COG0139.
HOGENOMi HOG000277504.
KOi K01496.
OrthoDBi EOG6PGKB6.

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00008 .

Family and domain databases

HAMAPi MF_01021. HisI.
InterProi IPR026660. PRA-CH.
IPR002496. PRib_AMP_CycHydrolase_dom.
[Graphical view ]
Pfami PF01502. PRA-CH. 1 hit.
[Graphical view ]
ProDomi PD002610. PRA_CycHdrlase. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1330.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1330.

Entry informationi

Entry nameiHIS3_BRUSU
AccessioniPrimary (citable) accession number: Q8G0L3
Secondary accession number(s): G0K9Z8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: November 7, 2003
Last modified: November 26, 2014
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Brucella suis
    Brucella suis (strain 1330): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3