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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Bifidobacterium longum (strain NCC 2705)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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)
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 sitei295NADUniRule annotation1
Metal bindingi349Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi351Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei352IMPUniRule annotation1
Active sitei354Thioimidate intermediateUniRule annotation1
Metal bindingi354Potassium; via carbonyl oxygenUniRule annotation1
Active sitei455Proton acceptorUniRule annotation1
Binding sitei470IMPUniRule annotation1
Metal bindingi524Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi525Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi526Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi347 – 349NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Potassium

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:BL1722
OrganismiBifidobacterium longum (strain NCC 2705)
Taxonomic identifieri206672 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaBifidobacterialesBifidobacteriaceaeBifidobacterium
Proteomesi
  • UP000000439 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004156881 – 545Inosine-5'-monophosphate dehydrogenaseAdd BLAST545

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi206672.BL1722.

Structurei

3D structure databases

ProteinModelPortaliQ8G3N6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini138 – 194CBS 1UniRule annotationAdd BLAST57
Domaini201 – 258CBS 2UniRule annotationAdd BLAST58

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni387 – 389IMP bindingUniRule annotation3
Regioni410 – 411IMP bindingUniRule annotation2
Regioni434 – 438IMP bindingUniRule annotation5

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiENOG4105CP4. Bacteria.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165755.
KOiK00088.
OMAiSSMGYCG.
PhylomeDBiQ8G3N6.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERiPTHR11911:SF6. PTHR11911:SF6. 2 hits.
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.

Q8G3N6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRCRTRQRIS ERSQACVVKV SACSYSVCMA TNLDELNAQS AYAPLPPIFA
60 70 80 90 100
KLGLAYDDVL LLPNETDVIP SEVDTSTHLT RKIVMKAPVL SAAMDTVTES
110 120 130 140 150
EMAIAMARNG GIGVLHRNLS IDDQAAQVDV VKRSESGMIT DPLTVNPEVT
160 170 180 190 200
LADLDKLCGK FHISGLPVVD KENKLVGIIT NRDMRFIASE DYDTLKVKDV
210 220 230 240 250
MTKENLVTGP SNISKDDAHR LLAQHKVEKL PLVDEEGHLT GLITVKDFVK
260 270 280 290 300
TEQYPDATKD EQGRLRVAAG VGFLGDAWQR ASALMEAGVD VLVVDTANGE
310 320 330 340 350
ARLALDMISR LKHDSAFDGV QIIGGNVGTR SGAQAMIEAG ADAVKVGIGP
360 370 380 390 400
GSICTTRIVA GVGVPQLTAV YEAAQACRAA GVPCIADGGI HYSGDIAKAL
410 420 430 440 450
VAGASSVMLG GTLAGCEEAP GEKVLLHGKQ YKLYRGMGSL GAMAPRGKKS
460 470 480 490 500
YSKDRYFQAD VTSSDKVVPE GVEGEVPYRG PLNAVLYQML GGLHQSMFYI
510 520 530 540
GAHNIAEMPE RGKFIRITDA GLRESHPHDI VMTTEAPNYS GFHNN
Length:545
Mass (Da):58,263
Last modified:March 1, 2003 - v1
Checksum:iE56CD074DAF63CD3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014295 Genomic DNA. Translation: AAN25506.1.
RefSeqiNP_696870.1. NC_004307.2.
WP_011068807.1. NC_004307.2.

Genome annotation databases

EnsemblBacteriaiAAN25506; AAN25506; BL1722.
GeneIDi1021976.
KEGGiblo:BL1722.
PATRICi21120714. VBIBifLon107831_1776.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014295 Genomic DNA. Translation: AAN25506.1.
RefSeqiNP_696870.1. NC_004307.2.
WP_011068807.1. NC_004307.2.

3D structure databases

ProteinModelPortaliQ8G3N6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi206672.BL1722.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN25506; AAN25506; BL1722.
GeneIDi1021976.
KEGGiblo:BL1722.
PATRICi21120714. VBIBifLon107831_1776.

Phylogenomic databases

eggNOGiENOG4105CP4. Bacteria.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165755.
KOiK00088.
OMAiSSMGYCG.
PhylomeDBiQ8G3N6.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERiPTHR11911:SF6. PTHR11911:SF6. 2 hits.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiIMDH_BIFLO
AccessioniPrimary (citable) accession number: Q8G3N6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 94 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.