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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: Annotation score: 4 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 sitei249NADUniRule annotation1
Metal bindingi301Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi303Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei304IMPUniRule annotation1
Active sitei306Thioimidate intermediateUniRule annotation1
Metal bindingi306Potassium; via carbonyl oxygenUniRule annotation1
Active sitei402Proton acceptorUniRule annotation1
Binding sitei416IMPUniRule annotation1
Metal bindingi470Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi471Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi472Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi249 – 251NADUniRule annotation3
Nucleotide bindingi299 – 301NADUniRule 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:HI_0221
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
Proteomesi
  • UP000000579 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000936971 – 488Inosine-5'-monophosphate dehydrogenaseAdd BLAST488

Proteomic databases

PRIDEiP44334.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi71421.HI0221.

Structurei

3D structure databases

ProteinModelPortaliP44334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini94 – 150CBS 1UniRule annotationAdd BLAST57
Domaini154 – 215CBS 2UniRule annotationAdd BLAST62

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni339 – 341IMP bindingUniRule annotation3
Regioni362 – 363IMP bindingUniRule annotation2
Regioni386 – 390IMP 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.
KOiK00088.
OMAiSSMGYCG.
PhylomeDBiP44334.

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.

P44334-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLRIKQEAL TFDDVLLVPA HSTVLPNTAN LSTQLTKEIR LNIPMLSAAM
60 70 80 90 100
DTVTETKLAI SLAQEGGIGF IHKNMTIERQ ADRVRKVKKF ESGIVSEPVT
110 120 130 140 150
VLPNLTLAEL AEMVKKNGFA GYPVVDGENN LIGIITGRDT RFVKDLSKTV
160 170 180 190 200
SQVMTKKEDL VTVKEGASRE EILELMHQHR VEKVLVVNDS FKLKGMITVK
210 220 230 240 250
DFQKAEQKPN ACKDEFGRLR VGAAVGAGAG NEERIDALVK AGVDVLLIDS
260 270 280 290 300
SHGHSEGVLQ RVRETRAKYP NLPIVAGNVA TAEGAIALAD AGASAVKVGI
310 320 330 340 350
GPGSICTTRI VTGVGVPQIT AIADAAAALK DRGIPVIADG GIRFSGDIAK
360 370 380 390 400
AIAAGASCVM VGSMFAGTEE APGEIELYQG RAFKSYRGMG SLGAMAKGSS
410 420 430 440 450
DRYFQSDNAA DKLVPEGIEG RIPYKGYLKE IIHQQMGGLR SCMGLTGCAT
460 470 480
IDELRTKAEF VRISGAGIKE SHVHDVAITK EAPNYRMG
Length:488
Mass (Da):51,981
Last modified:November 1, 1995 - v1
Checksum:iB477F22344E4BE8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC21890.1.
PIRiH64055.
RefSeqiNP_438392.1. NC_000907.1.
WP_005694071.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC21890; AAC21890; HI_0221.
GeneIDi951137.
KEGGihin:HI0221.
PATRICi20188961. VBIHaeInf48452_0233.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC21890.1.
PIRiH64055.
RefSeqiNP_438392.1. NC_000907.1.
WP_005694071.1. NC_000907.1.

3D structure databases

ProteinModelPortaliP44334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi71421.HI0221.

Proteomic databases

PRIDEiP44334.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC21890; AAC21890; HI_0221.
GeneIDi951137.
KEGGihin:HI0221.
PATRICi20188961. VBIHaeInf48452_0233.

Phylogenomic databases

eggNOGiENOG4105CP4. Bacteria.
COG0516. LUCA.
COG0517. LUCA.
KOiK00088.
OMAiSSMGYCG.
PhylomeDBiP44334.

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_HAEIN
AccessioniPrimary (citable) accession number: P44334
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 126 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. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.