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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: 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.
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

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-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciBSUB:BSU06520-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
Synonyms:purHJ
Ordered Locus Names:BSU06520
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU06520. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 512512Bifunctional purine biosynthesis protein PurHPRO_0000192070Add
BLAST

Proteomic databases

PaxDbiP12048.

Interactioni

Protein-protein interaction databases

IntActiP12048. 1 interaction.
MINTiMINT-8364997.
STRINGi224308.BSU06520.

Structurei

3D structure databases

ProteinModelPortaliP12048.
SMRiP12048. Positions 2-512.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.Curated

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230372.
InParanoidiP12048.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.
PhylomeDBiP12048.

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.

P12048-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIKRALISV SDKTNLVPFV KELTELGVEV ISTGGTKKLL QENGVDVIGI
60 70 80 90 100
SEVTGFPEIM DGRLKTLHPN IHGGLLAVRG NEEHMAQINE HGIQPIDLVV
110 120 130 140 150
VNLYPFKETI SKEDVTYEEA IENIDIGGPG MLRAASKNHQ DVTVIVDPAD
160 170 180 190 200
YSPVLNQIKE EGSVSLQKKR ELAAKVFRHT AAYDALIADY LTNVVGEKEP
210 220 230 240 250
EQFTVTFEKK QSLRYGENPH QEATFYQTAL PVKGSIAQAE QLHGKELSYN
260 270 280 290 300
NIKDADAAVQ IVREFTEPAA VAVKHMNPCG VGTGKTIAEA FDRAFEADKT
310 320 330 340 350
SIFGGIIALN REVDKATAEA LHNIFLEIII APSFSQEALD VLTAKKNLRL
360 370 380 390 400
LTLDVSAAVQ KEKQLTSVQG GLLIQDLDMH GFDDAEISIP TKREPNEQEW
410 420 430 440 450
EDLKLAWKVV KHVKSNAIVL AKDNMTVGVG AGQMNRVGSA KIAIEQAGEK
460 470 480 490 500
AKGSALGSDA YFPMPDTVEE AAKAGVTAII QPGGSIRDED SIKKADEYGI
510
AMVFTGIRHF KH
Length:512
Mass (Da):55,753
Last modified:July 7, 2009 - v2
Checksum:i832CE152D9CEC358
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti351 – 3511L → V in AAA22683 (PubMed:3036807).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02732 Genomic DNA. Translation: AAA22683.1.
AL009126 Genomic DNA. Translation: CAB12472.2.
AF011544 Genomic DNA. Translation: AAB72185.1.
PIRiA29183. DTBSPH.
RefSeqiNP_388534.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12472; CAB12472; BSU06520.
GeneIDi936053.
KEGGibsu:BSU06520.
PATRICi18972946. VBIBacSub10457_0687.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02732 Genomic DNA. Translation: AAA22683.1.
AL009126 Genomic DNA. Translation: CAB12472.2.
AF011544 Genomic DNA. Translation: AAB72185.1.
PIRiA29183. DTBSPH.
RefSeqiNP_388534.2. NC_000964.3.

3D structure databases

ProteinModelPortaliP12048.
SMRiP12048. Positions 2-512.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP12048. 1 interaction.
MINTiMINT-8364997.
STRINGi224308.BSU06520.

Proteomic databases

PaxDbiP12048.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12472; CAB12472; BSU06520.
GeneIDi936053.
KEGGibsu:BSU06520.
PATRICi18972946. VBIBacSub10457_0687.

Organism-specific databases

GenoListiBSU06520. [Micado]

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230372.
InParanoidiP12048.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.
PhylomeDBiP12048.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciBSUB:BSU06520-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis."
    Ebbole D.J., Zalkin H.
    J. Biol. Chem. 262:8274-8287(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 351.
  4. "The 52 degrees-55 degrees segment of the Bacillus subtilis chromosome: a region devoted to purine uptake and metabolism, and containing the genes cotA, gabP and guaA and the pur gene cluster within a 34960 bp nucleotide sequence."
    Borriss R., Porwollik S., Schroeter R.
    Microbiology 142:3027-3031(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 432-512.
    Strain: 168.

Entry informationi

Entry nameiPUR9_BACSU
AccessioniPrimary (citable) accession number: P12048
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 7, 2009
Last modified: January 7, 2015
This is version 114 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, Multifunctional enzyme, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.