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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Unreviewed-Annotation score: 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: XMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Inosine-5'-monophosphate dehydrogenase (guaB), Inosine-5'-monophosphate dehydrogenase (guaB)
This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei244NADUniRule annotation1
Metal bindingi296Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi298Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei299IMPUniRule annotation1
Active sitei301Thioimidate intermediateUniRule annotation1
Metal bindingi301Potassium; via carbonyl oxygenUniRule annotation1
Active sitei397Proton acceptorUniRule annotation1
Binding sitei409IMPUniRule annotation1
Metal bindingi463Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi464Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi465Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi294 – 296NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductaseUniRule annotation
Biological processGMP biosynthesisUniRule annotation, Purine biosynthesis
LigandMetal-bindingUniRule annotation, NADUniRule annotation, PotassiumUniRule annotation

Enzyme and pathway databases

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
Gene namesi
Name:guaBUniRule annotation
Ordered Locus Names:TM_1347Imported
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)Imported
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi243274.TM1347.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VRDX-ray2.18A/B1-482[»]
SMRiQ9X168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni334 – 336IMP bindingUniRule annotation3
Regioni357 – 358IMP bindingUniRule annotation2
Regioni381 – 385IMP bindingUniRule annotation5

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation

Keywords - Domaini

CBS domainPROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105CP4. Bacteria.
COG0516. LUCA.
COG0517. LUCA.
KOiK00088.
OMAiGIGIVHK.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
PfamiView protein in Pfam
PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
PIRSFiPIRSF000130. IMPDH. 1 hit.
SMARTiView protein in SMART
SM00116. CBS. 2 hits.
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiView protein in PROSITE
PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9X168-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKEALTFDDV LLVPQYSEVL PKDVKIDTRL TRQIRINIPL VSAAMDTVTE
60 70 80 90 100
AALAKALARE GGIGIIHKNL TPDEQARQVS IVKKTENGII YDPITVTPDM
110 120 130 140 150
TVKEAIDLMA EYKIGGLPVV DEEGRLVGLL TNRDVRFEKN LSKKIKDLMT
160 170 180 190 200
PREKLIVAPP DISLEKAKEI LHQHRIEKLP LVSKDNKLVG LITIKDIMSV
210 220 230 240 250
IEHPNAARDE KGRLLVGAAV GTSPETMERV EKLVKAGVDV IVIDTAHGHS
260 270 280 290 300
RRVIETLEMI KADYPDLPVV AGNVATPEGT EALIKAGADA VKVGVGPGSI
310 320 330 340 350
CTTRVVAGVG VPQLTAVMEC SEVARKYDVP IIADGGIRYS GDIVKALAAG
360 370 380 390 400
AESVMVGSIF AGTEEAPGET ILYQGRKYKA YRGMGSLGAM RSGSADRYGQ
410 420 430 440 450
EGENKFVPEG IEGMVPYKGT VKDVVHQLVG GLRSGMGYIG ARTIKELQEK
460 470 480
AVFVKITPAG VKESHPHDII ITKESPNYWV QA
Length:482
Mass (Da):52,014
Last modified:November 1, 1999 - v1
Checksum:i4E08237F69D909FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36418.1.
PIRiC72264.
RefSeqiNP_229148.1. NC_000853.1.
WP_004081543.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD36418; AAD36418; TM_1347.
AGL50278; AGL50278; Tmari_1354.
GeneIDi29652887.
898133.
KEGGitma:TM1347.
tmi:THEMA_07605.
tmm:Tmari_1354.
tmw:THMA_1372.
PATRICifig|243274.17.peg.1354.

Similar proteinsi

Entry informationi

Entry nameiQ9X168_THEMA
AccessioniPrimary (citable) accession number: Q9X168
Secondary accession number(s): G4FF83
Entry historyiIntegrated into UniProtKB/TrEMBL: November 1, 1999
Last sequence update: November 1, 1999
Last modified: August 30, 2017
This is version 128 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported