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Q9KV80

- PUR9_VIBCH

UniProt

Q9KV80 - PUR9_VIBCH

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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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: TIGR

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciVCHO:VC0276-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:VC_0276
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000000584: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 530530Bifunctional purine biosynthesis protein PurHPRO_0000192144Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243277.VC0276.

Structurei

3D structure databases

ProteinModelPortaliQ9KV80.
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.
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.

Q9KV80-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNNARPIHRA LLSVSDKTGI VEFAKALAER GVELLSTGGT ARLLAEQGLT
60 70 80 90 100
VTEVSDYTGF PEMMDGRVKT LHPKVHGGIL GRRGQDDAVM NTHGIQPIDM
110 120 130 140 150
VVVNLYPFAQ TVANPNCTLA DAVENIDIGG PTMVRSAAKN HKDVAIVVNA
160 170 180 190 200
HDYDRVIREM DANHNSLTLA TRFDLAIAAF EHTAAYDGMI ANYFGTLVPS
210 220 230 240 250
YGDNKEGDEE SKFPRTFNAQ FIKKQDMRYG ENSHQAAAFY VEANPQEASV
260 270 280 290 300
ATARQIQGKA LSYNNIADTD AALECVKEFS EPACVIVKHA NPCGVALGDD
310 320 330 340 350
LLQAYNRAYQ TDPTSAFGGI IAFNRELDGE TARAIIERQF VEVIIAPKVS
360 370 380 390 400
QAAIDIVAAK QNVRLLECGE WQGQTTGFDL KRVNGGLLVQ DRDQGMVAQD
410 420 430 440 450
DLQVVSTRQP SDAELKDALF CWKVAKYVKS NAIVYAKGDM TIGIGAGQMS
460 470 480 490 500
RVYSAKIAGI KAADEGLEVA GSVMASDAFF PFRDGIDAAA EAGITCVIQP
510 520 530
GGSMRDQEVI DAANEHGMAM IFTGMRHFRH
Length:530
Mass (Da):57,327
Last modified:October 1, 2000 - v1
Checksum:iBE64A6D4C42FA617
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF93451.1.
PIRiC82344.
RefSeqiNP_229932.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF93451; AAF93451; VC_0276.
GeneIDi2614999.
KEGGivch:VC0276.
PATRICi20079595. VBIVibCho83274_0256.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF93451.1 .
PIRi C82344.
RefSeqi NP_229932.1. NC_002505.1.

3D structure databases

ProteinModelPortali Q9KV80.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243277.VC0276.

Protocols and materials databases

DNASUi 2614999.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF93451 ; AAF93451 ; VC_0276 .
GeneIDi 2614999.
KEGGi vch:VC0276.
PATRICi 20079595. VBIVibCho83274_0256.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
BioCyci VCHO:VC0276-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 39315 / El Tor Inaba N16961.

Entry informationi

Entry nameiPUR9_VIBCH
AccessioniPrimary (citable) accession number: Q9KV80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: October 1, 2000
Last modified: October 1, 2014
This is version 79 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