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Q0I557

- PUR9_HISS1

UniProt

Q0I557 - PUR9_HISS1

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Protein

Bifunctional purine biosynthesis protein PurH

Gene
purH, HS_1625
Organism
Histophilus somni (strain 129Pt) (Haemophilus somnus)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. IMP cyclohydrolase activity Source: UniProtKB-HAMAP
  2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciHSOM205914:GJ7V-1706-MONOMER.
UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PurH
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC:2.1.2.3)
Alternative name(s):
AICAR transformylase
IMP cyclohydrolase (EC:3.5.4.10)
Alternative name(s):
ATIC
IMP synthase
Inosinicase
Gene namesi
Name:purH
Ordered Locus Names:HS_1625
OrganismiHistophilus somni (strain 129Pt) (Haemophilus somnus)
Taxonomic identifieri205914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus
ProteomesiUP000001970: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 532532Bifunctional purine biosynthesis protein PurHUniRule annotationPRO_1000018892Add
BLAST

Proteomic databases

PRIDEiQ0I557.

Interactioni

Protein-protein interaction databases

STRINGi205914.HS_1625.

Structurei

3D structure databases

ProteinModelPortaliQ0I557.

Family & Domainsi

Domaini

The IMP cyclohydrolase activity resides in the N-terminal region By similarity.UniRule annotation

Sequence similaritiesi

Belongs to the PurH family.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230372.
KOiK00602.
OrthoDBiEOG6QCDFF.

Family and domain databases

Gene3Di3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.

Sequencei

Sequence statusi: Complete.

Q0I557-1 [UniParc]FASTAAdd to Basket

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MQLNHPIRQA LLSVSDKSGI VEFAQGLVKR GVKLLSTGGT AKLLAENGIP    50
VTEVSDYTGF PEMMEGRVKT LHPKIHGGIL GRRGIDDEVM MQHQIDAIDM 100
VVVNLYPFAA TVAKPDCTLE DAVENIDIGG PTMVRSAAKN HQHVAIVVNN 150
SDFNAILAEM DQNRNSLTLE TRFDLAIKAF EHTAQYDSMI ANYFGQMVKP 200
YFRAEEEAEA KCGQFPRTLN LNFIRKQSMR YGENGHQKAA FYVEQDVKEA 250
SVSTAKQLQG KALSYNNIAD TDAALECVKS FSEPACVIVK HANPCGVALG 300
KDILEAYNRA YQTDPTSAFG GIIAFNRELD EDTAKAIIER QFVEVIIAPT 350
VSSAAQEIVK SKKNVRLLTC GNWESAIQRL DFKRVNGGLL VQEADLSMVD 400
LADLEVVSKR QPTKQELEDL LFCWKVAKFV KSNAIVYAKN NQTVGIGAGQ 450
MSRVYSAKIA GIKAKDEGLE VKGCVMASDA FFPFRDGIDA AAKVGIECVI 500
HPGGSMRDQE VIDAANEHNM VMVLTKMRHF RH 532
Length:532
Mass (Da):58,521
Last modified:October 3, 2006 - v1
Checksum:iB4B1BE8963C9161C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000436 Genomic DNA. Translation: ABI25893.1.
RefSeqiWP_011609771.1. NC_008309.1.
YP_719830.1. NC_008309.1.

Genome annotation databases

EnsemblBacteriaiABI25893; ABI25893; HS_1625.
GeneIDi4241152.
KEGGihso:HS_1625.
PATRICi20283407. VBIHaeSom53361_1703.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000436 Genomic DNA. Translation: ABI25893.1 .
RefSeqi WP_011609771.1. NC_008309.1.
YP_719830.1. NC_008309.1.

3D structure databases

ProteinModelPortali Q0I557.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 205914.HS_1625.

Proteomic databases

PRIDEi Q0I557.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABI25893 ; ABI25893 ; HS_1625 .
GeneIDi 4241152.
KEGGi hso:HS_1625.
PATRICi 20283407. VBIHaeSom53361_1703.

Phylogenomic databases

eggNOGi COG0138.
HOGENOMi HOG000230372.
KOi K00602.
OrthoDBi EOG6QCDFF.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
BioCyci HSOM205914:GJ7V-1706-MONOMER.

Family and domain databases

Gene3Di 3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPi MF_00139. PurH.
InterProi IPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view ]
PANTHERi PTHR11692. PTHR11692. 1 hit.
Pfami PF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view ]
PIRSFi PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTi SM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsi TIGR00355. purH. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
    Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
    J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 129Pt.

Entry informationi

Entry nameiPUR9_HISS1
AccessioniPrimary (citable) accession number: Q0I557
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: September 3, 2014
This is version 60 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, Multifunctional enzyme

Documents

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

External Data

Dasty 3

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