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P21879

- IMDH_BACSU

UniProt

P21879 - IMDH_BACSU

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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

Cofactori

K(+)UniRule annotation

Enzyme regulationi

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.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei251 – 2511NADUniRule annotation
Metal bindingi303 – 3031Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi305 – 3051Potassium; via carbonyl oxygenUniRule annotation
Binding sitei306 – 3061IMPUniRule annotation
Active sitei308 – 3081Thioimidate intermediateUniRule annotation
Metal bindingi308 – 3081Potassium; via carbonyl oxygenUniRule annotation
Binding sitei416 – 4161IMPUniRule annotation
Metal bindingi470 – 4701Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi471 – 4711Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi472 – 4721Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi301 – 3033NADUniRule annotation

GO - Molecular functioni

  1. adenyl nucleotide binding Source: InterPro
  2. IMP dehydrogenase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. GMP biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Potassium

Enzyme and pathway databases

BioCyciBSUB:BSU00090-MONOMER.
UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation)
Short name:
IMP dehydrogenaseUniRule annotation
Short name:
IMPDUniRule annotation
Short name:
IMPDHUniRule annotation
Alternative name(s):
Superoxide-inducible protein 12
Short name:
SOI12
Gene namesi
Name:guaBUniRule annotation
Synonyms:gnaB
Ordered Locus Names:BSU00090
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU00090. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 488488Inosine-5'-monophosphate dehydrogenasePRO_0000093691Add
BLAST

Proteomic databases

PaxDbiP21879.
PRIDEiP21879.

Expressioni

Inductioni

By superoxide.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

IntActiP21879. 1 interaction.
MINTiMINT-8365336.
STRINGi224308.BSU00090.

Structurei

3D structure databases

ProteinModelPortaliP21879.
SMRiP21879. Positions 2-486.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 15359CBS 1UniRule annotationAdd
BLAST
Domaini157 – 21458CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni341 – 3433IMP bindingUniRule annotation
Regioni364 – 3652IMP bindingUniRule annotation
Regioni388 – 3925IMP bindingUniRule annotation

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation
Contains 2 CBS domains.UniRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
HOGENOMiHOG000165754.
InParanoidiP21879.
KOiK00088.
OMAiHGHSKNI.
OrthoDBiEOG6GTZPV.
PhylomeDBiP21879.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PfamiPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000130. IMPDH. 1 hit.
SMARTiSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21879-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MWESKFSKEG LTFDDVLLVP AKSEVLPRDV DLSVELTKTL KLNIPVISAG
60 70 80 90 100
MDTVTESAMA IAMARQGGLG IIHKNMSIEQ QAEQVDKVKR SERGVITNPF
110 120 130 140 150
FLTPDHQVFD AEHLMGKYRI SGVPIVNNEE DQKLVGIITN RDLRFISDYS
160 170 180 190 200
MKISDVMTKE ELVTASVGTT LDEAEKILQK HKIEKLPLVD DQNKLKGLIT
210 220 230 240 250
IKDIEKVIEF PNSSKDIHGR LIVGAAVGVT GDTMTRVKKL VEANVDVIVI
260 270 280 290 300
DTAHGHSQGV LNTVTKIRET YPELNIIAGN VATAEATRAL IEAGADVVKV
310 320 330 340 350
GIGPGSICTT RVVAGVGVPQ ITAIYDCATE ARKHGKTIIA DGGIKFSGDI
360 370 380 390 400
TKALAAGGHA VMLGSLLAGT SESPGETEIY QGRRFKVYRG MGSVAAMEKG
410 420 430 440 450
SKDRYFQEEN KKFVPEGIEG RTPYKGPVEE TVYQLVGGLR SGMGYCGSKD
460 470 480
LRALREEAQF IRMTGAGLRE SHPHDVQITK ESPNYTIS
Length:488
Mass (Da):52,991
Last modified:August 29, 2003 - v2
Checksum:i34939E2758EA48B6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281R → H in CAA39204. (PubMed:1979163)Curated
Sequence conflicti480 – 4889KESPNYTIS → VHRNKALPGLFGSHQKKTGF VYDECCQSGFFSSD in CAA39204. (PubMed:1979163)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55669 Genomic DNA. Translation: CAA39204.1.
D26185 Genomic DNA. Translation: BAA05245.1.
AL009126 Genomic DNA. Translation: CAB11785.1.
PIRiS66039. DEBSMP.
RefSeqiNP_387890.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB11785; CAB11785; BSU00090.
GeneIDi938032.
KEGGibsu:BSU00090.
PATRICi18971477. VBIBacSub10457_0010.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55669 Genomic DNA. Translation: CAA39204.1 .
D26185 Genomic DNA. Translation: BAA05245.1 .
AL009126 Genomic DNA. Translation: CAB11785.1 .
PIRi S66039. DEBSMP.
RefSeqi NP_387890.1. NC_000964.3.

3D structure databases

ProteinModelPortali P21879.
SMRi P21879. Positions 2-486.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P21879. 1 interaction.
MINTi MINT-8365336.
STRINGi 224308.BSU00090.

Proteomic databases

PaxDbi P21879.
PRIDEi P21879.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB11785 ; CAB11785 ; BSU00090 .
GeneIDi 938032.
KEGGi bsu:BSU00090.
PATRICi 18971477. VBIBacSub10457_0010.

Organism-specific databases

GenoListi BSU00090. [Micado ]

Phylogenomic databases

eggNOGi COG0517.
HOGENOMi HOG000165754.
InParanoidi P21879.
KOi K00088.
OMAi HGHSKNI.
OrthoDBi EOG6GTZPV.
PhylomeDBi P21879.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
BioCyci BSUB:BSU00090-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01964. IMPDH.
InterProi IPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view ]
Pfami PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000130. IMPDH. 1 hit.
SMARTi SM00116. CBS. 2 hits.
[Graphical view ]
TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
PROSITEi PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiIMDH_BACSU
AccessioniPrimary (citable) accession number: P21879
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: August 29, 2003
Last modified: November 26, 2014
This is version 131 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, Direct protein sequencing, 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