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P21879 (IMDH_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inosine-5'-monophosphate dehydrogenase

Short name=IMP dehydrogenase
Short name=IMPD
Short name=IMPDH
EC=1.1.1.205
Alternative name(s):
Superoxide-inducible protein 12
Short name=SOI12
Gene names
Name:guaB
Synonyms:gnaB
Ordered Locus Names:BSU00090
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth By similarity. HAMAP-Rule MF_01964

Catalytic activity

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH. HAMAP-Rule MF_01964

Cofactor

Potassium By similarity. HAMAP-Rule MF_01964

Enzyme regulation

Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH By similarity. HAMAP-Rule MF_01964

Pathway

Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. HAMAP-Rule MF_01964

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01964

Induction

By superoxide. HAMAP-Rule MF_01964

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093691

Regions

Domain95 – 15359CBS 1
Domain157 – 21458CBS 2
Nucleotide binding301 – 3033NAD By similarity
Region341 – 3433IMP binding By similarity
Region364 – 3652IMP binding By similarity
Region388 – 3925IMP binding By similarity

Sites

Active site3081Thioimidate intermediate By similarity
Metal binding3031Potassium; via carbonyl oxygen By similarity
Metal binding3051Potassium; via carbonyl oxygen By similarity
Metal binding3081Potassium; via carbonyl oxygen By similarity
Metal binding4701Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4711Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4721Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2511NAD By similarity
Binding site3061IMP By similarity
Binding site4161IMP By similarity

Experimental info

Sequence conflict281R → H in CAA39204. Ref.1
Sequence conflict480 – 4889KESPNYTIS → VHRNKALPGLFGSHQKKTGF VYDECCQSGFFSSD in CAA39204. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P21879 [UniParc].

Last modified August 29, 2003. Version 2.
Checksum: 34939E2758EA48B6

FASTA48852,991
        10         20         30         40         50         60 
MWESKFSKEG LTFDDVLLVP AKSEVLPRDV DLSVELTKTL KLNIPVISAG MDTVTESAMA 

        70         80         90        100        110        120 
IAMARQGGLG IIHKNMSIEQ QAEQVDKVKR SERGVITNPF FLTPDHQVFD AEHLMGKYRI 

       130        140        150        160        170        180 
SGVPIVNNEE DQKLVGIITN RDLRFISDYS MKISDVMTKE ELVTASVGTT LDEAEKILQK 

       190        200        210        220        230        240 
HKIEKLPLVD DQNKLKGLIT IKDIEKVIEF PNSSKDIHGR LIVGAAVGVT GDTMTRVKKL 

       250        260        270        280        290        300 
VEANVDVIVI DTAHGHSQGV LNTVTKIRET YPELNIIAGN VATAEATRAL IEAGADVVKV 

       310        320        330        340        350        360 
GIGPGSICTT RVVAGVGVPQ ITAIYDCATE ARKHGKTIIA DGGIKFSGDI TKALAAGGHA 

       370        380        390        400        410        420 
VMLGSLLAGT SESPGETEIY QGRRFKVYRG MGSVAAMEKG SKDRYFQEEN KKFVPEGIEG 

       430        440        450        460        470        480 
RTPYKGPVEE TVYQLVGGLR SGMGYCGSKD LRALREEAQF IRMTGAGLRE SHPHDVQITK 


ESPNYTIS 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the Bacillus subtilis IMP dehydrogenase gene."
Kanzaki N., Miyagawa K.I.
Nucleic Acids Res. 18:6710-6710(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
Ogasawara N., Nakai S., Yoshikawa H.
DNA Res. 1:1-14(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"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. expand/collapse author list , 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.
[4]"First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis."
Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.
Electrophoresis 18:1451-1463(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-25.
Strain: 168 / IS58.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X55669 Genomic DNA. Translation: CAA39204.1.
D26185 Genomic DNA. Translation: BAA05245.1.
AL009126 Genomic DNA. Translation: CAB11785.1.
PIRDEBSMP. S66039.
RefSeqNP_387890.1. NC_000964.3.

3D structure databases

ProteinModelPortalP21879.
SMRP21879. Positions 2-486.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP21879. 1 interaction.
MINTMINT-8365336.
STRING224308.BSU00090.

Proteomic databases

PaxDbP21879.
PRIDEP21879.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB11785; CAB11785; BSU00090.
GeneID938032.
KEGGbsu:BSU00090.
PATRIC18971477. VBIBacSub10457_0010.

Organism-specific databases

GenoListBSU00090. [Micado]

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165754.
KOK00088.
OMAHGHSKNI.
OrthoDBEOG6GTZPV.
PhylomeDBP21879.

Enzyme and pathway databases

BioCycBSUB:BSU00090-MONOMER.
UniPathwayUPA00601; UER00295.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PfamPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF000130. IMPDH. 1 hit.
SMARTSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsTIGR01302. IMP_dehydrog. 1 hit.
PROSITEPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIMDH_BACSU
AccessionPrimary (citable) accession number: P21879
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: August 29, 2003
Last modified: July 9, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList