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Q89B23

- PUR9_BUCBP

UniProt

Q89B23 - PUR9_BUCBP

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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
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

BioCyciBAPH224915:GJ9D-32-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:bbp_032
OrganismiBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Taxonomic identifieri224915 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000000601: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Bifunctional purine biosynthesis protein PurHPRO_0000192078Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi224915.bbp032.

Structurei

3D structure databases

ProteinModelPortaliQ89B23.
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.
KOiK00602.
OMAiCGVATGP.
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.

Q89B23-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTNRNVIKNV LISVSDTSNI IEFSKSLISK NIKLFATKGT ANFLKKNNIY
60 70 80 90 100
ATDITNYTNF PEIMNGRIKT LHHKIYASIL AQPKHDKKTI EKYNIILMDI
110 120 130 140 150
VVINFYPFEE ASNNTNLHLN DIIEHIDIGG PAIVRAAAKN YKNVLVVTQP
160 170 180 190 200
NLYQSIVNEM NLNNNIISET TKLKFATIAF KHTMNYDNNI YQYLSKKNKT
210 220 230 240 250
VPKNTQLQTL LPSHLTINFK KKQDLCYGEN KQQQASWYTN TSKNTSGRMK
260 270 280 290 300
IKQLQGKILS YNNLSDIHLA LSCIHEFNKT TCAIIKHGNP CGVATAKNND
310 320 330 340 350
QAYKLAYETD PISAFGGIIV FNQKLNDVTA RKIIKTQFSE IILAPDFTQE
360 370 380 390 400
AKKIFDKKPN LRIIKYDPNY NYLNYNIDIK SIYGDILVQS NTNSIININQ
410 420 430 440 450
WDIVSKKRPN EQEINDAKFA LRVVKHLKSN SIVLIKNQIT ISIGSGQTSR
460 470 480 490 500
IDATKIAIYK ANNNNISLNH TTLASDAFFP FSDSIDLISK SGITCIVQPG
510 520
GSIRDNEIIM SANKYNISMI FTKQRYFKH
Length:529
Mass (Da):60,084
Last modified:June 20, 2003 - v1
Checksum:i940058B815B31047
GO

Sequence cautioni

The sequence AAO26775.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016826 Genomic DNA. Translation: AAO26775.1. Different initiation.
RefSeqiNP_777670.1. NC_004545.1.

Genome annotation databases

EnsemblBacteriaiAAO26775; AAO26775; bbp_032.
GeneIDi1058351.
KEGGibab:bbp032.
PATRICi21244835. VBIBucAph80364_0032.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016826 Genomic DNA. Translation: AAO26775.1 . Different initiation.
RefSeqi NP_777670.1. NC_004545.1.

3D structure databases

ProteinModelPortali Q89B23.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224915.bbp032.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO26775 ; AAO26775 ; bbp_032 .
GeneIDi 1058351.
KEGGi bab:bbp032.
PATRICi 21244835. VBIBucAph80364_0032.

Phylogenomic databases

eggNOGi COG0138.
KOi K00602.
OMAi CGVATGP.
OrthoDBi EOG6QCDFF.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
BioCyci BAPH224915:GJ9D-32-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: Bp.

Entry informationi

Entry nameiPUR9_BUCBP
AccessioniPrimary (citable) accession number: Q89B23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: October 1, 2014
This is version 75 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