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Q6G5S5

- PUR9_BARHE

UniProt

Q6G5S5 - PUR9_BARHE

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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Bartonella henselae (strain ATCC 49882 / Houston 1) (Rochalimaea henselae)
Status
Reviewed - Annotation score: 2 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

BioCyciBHEN283166:GIVZ-1592-MONOMER.
UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PurHUniRule annotation
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferaseUniRule annotation (EC:2.1.2.3UniRule annotation)
Alternative name(s):
AICAR transformylaseUniRule annotation
IMP cyclohydrolaseUniRule annotation (EC:3.5.4.10UniRule annotation)
Alternative name(s):
ATICUniRule annotation
IMP synthaseUniRule annotation
InosinicaseUniRule annotation
Gene namesi
Name:purHUniRule annotation
Ordered Locus Names:BH15970
OrganismiBartonella henselae (strain ATCC 49882 / Houston 1) (Rochalimaea henselae)
Taxonomic identifieri283166 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella
ProteomesiUP000000421: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 538538Bifunctional purine biosynthesis protein PurHPRO_1000018845Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi283166.BH15970.

Structurei

3D structure databases

ProteinModelPortaliQ6G5S5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230373.
KOiK00602.
OMAiRAFKTDP.
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.

Q6G5S5 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGVVAKNFPI PDLHRVRRVL LSVSDKTGIV AFAQALQTYN VELISTGGTA
60 70 80 90 100
KVLMAAGLPV RDVAEVTGFP EIMDGRVKTL HPLIHGALLG VREDPSHAVA
110 120 130 140 150
MEQYGIHGID LLVVNLYPFE ETVQSGADGQ TILENIDIGG PAMIRAAAKN
160 170 180 190 200
HVYTGVITAV SDYDAVLSEL KQHDGCLSFS MRQQLAMRAY AHTAAYDTAI
210 220 230 240 250
AAWFAKNLKI ETPSWQSFSG HLKNVMRYGE NPHQKAAFYR NGDKRFGVAT
260 270 280 290 300
AKLLQGKALS YNNMNDTDAA FELVAEFDPQ NTAAVALIKH ANPCGVAEGQ
310 320 330 340 350
TLKEAYLKAL LCDNVSAFGG IIALNQPLDA ECAEEVIKIF TEVIIAPDAT
360 370 380 390 400
MEAREIISGK KNLRLLLTGG VPDPRCGGFI AKTLAGGILV QSRDNVVVDD
410 420 430 440 450
LKLQVVTKRA PSQEEMRDLQ FAFRVVKHVK SNAIVYAKNS ATVGIGAGQM
460 470 480 490 500
SRVDSAKIAA RKAEESAKRA GLTESLTKGS VVASDAFFPF ADGLLAVAEA
510 520 530
GATAVIQPGG SMRDEEVIAA ADAQGLAMVF TGVRHFRH
Length:538
Mass (Da):57,597
Last modified:July 19, 2004 - v1
Checksum:i297641A8121EB54F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX897699 Genomic DNA. Translation: CAF28360.1.
RefSeqiYP_034290.1. NC_005956.1.

Genome annotation databases

EnsemblBacteriaiCAF28360; CAF28360; BH15970.
GeneIDi2864772.
KEGGibhe:BH15970.
PATRICi20547496. VBIBarHen29080_1856.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX897699 Genomic DNA. Translation: CAF28360.1 .
RefSeqi YP_034290.1. NC_005956.1.

3D structure databases

ProteinModelPortali Q6G5S5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 283166.BH15970.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAF28360 ; CAF28360 ; BH15970 .
GeneIDi 2864772.
KEGGi bhe:BH15970.
PATRICi 20547496. VBIBarHen29080_1856.

Phylogenomic databases

eggNOGi COG0138.
HOGENOMi HOG000230373.
KOi K00602.
OMAi RAFKTDP.
OrthoDBi EOG6QCDFF.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
BioCyci BHEN283166:GIVZ-1592-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49882 / Houston 1.

Entry informationi

Entry nameiPUR9_BARHE
AccessioniPrimary (citable) accession number: Q6G5S5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 19, 2004
Last modified: October 29, 2014
This is version 64 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, 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