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Q1MQT2 (Q1MQT2_LAWIP) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
Short name=IMP dehydrogenase HAMAP-Rule MF_01964
Short name=IMPD HAMAP-Rule MF_01964
Short name=IMPDH HAMAP-Rule MF_01964
EC=1.1.1.205 HAMAP-Rule MF_01964
Gene names
Name:guaB HAMAP-Rule MF_01964 EMBL CAJ54645.1
Ordered Locus Names:LI0591 EMBL CAJ54645.1
OrganismLawsonia intracellularis (strain PHE/MN1-00) [Complete proteome] [HAMAP] EMBL CAJ54645.1
Taxonomic identifier363253 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Lawsonia ›

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. RuleBase RU003928 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. RuleBase RU003928 HAMAP-Rule MF_01964

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01964

Sequence similarities

Belongs to the IMPDH/GMPR family. RuleBase RU003927 HAMAP-Rule MF_01964

Contains 2 CBS domains. HAMAP-Rule MF_01964

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain98 – 15760CBS 1 By similarity HAMAP-Rule MF_01964
Domain158 – 21558CBS 2 By similarity HAMAP-Rule MF_01964
Nucleotide binding302 – 3043NAD By similarity HAMAP-Rule MF_01964
Region342 – 3443IMP binding By similarity HAMAP-Rule MF_01964
Region365 – 3662IMP binding By similarity HAMAP-Rule MF_01964
Region389 – 3935IMP binding By similarity HAMAP-Rule MF_01964

Sites

Active site3091Thioimidate intermediate By similarity PIRSR PIRSR000130-1 HAMAP-Rule MF_01964
Metal binding3041Potassium; via carbonyl oxygen By similarity HAMAP-Rule MF_01964
Metal binding3061Potassium; via carbonyl oxygen By similarity HAMAP-Rule MF_01964
Metal binding3091Potassium; via carbonyl oxygen By similarity HAMAP-Rule MF_01964
Metal binding4711Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity HAMAP-Rule MF_01964
Metal binding4721Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity HAMAP-Rule MF_01964
Metal binding4731Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity HAMAP-Rule MF_01964
Binding site2521NAD By similarity HAMAP-Rule MF_01964
Binding site3071IMP By similarity HAMAP-Rule MF_01964
Binding site4171IMP By similarity HAMAP-Rule MF_01964

Sequences

Sequence LengthMass (Da)Tools
Q1MQT2 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 1B6305C988774867

FASTA49152,827
        10         20         30         40         50         60 
MNQDITNKIR YKALTFDDVL LIPAYSEVTP DKVNISAWLT PSLLLSIPFI SAAMDTVTES 

        70         80         90        100        110        120 
AMAISMARAG GIGIIHKNMS ISRQKMEVEK VKKSENGMIL DPVTVRPEDT VEHALELMQL 

       130        140        150        160        170        180 
YRVSGLPVVQ DKTLIGIVTN RDVRFVEDLS NTFVHEVMTR ENLVTVPVGT TLDEAKHHLH 

       190        200        210        220        230        240 
MHRIEKLLVV NEAGQLAGLL TMKDIDKIQK YPNACKDDKG RLCVGAAIGV GSDCEARAEA 

       250        260        270        280        290        300 
LLMAGVDVLV LDSAHGHSKN ILHAVKVIKH SFPNCQLIAG NVATYEAAKS LLLAGADAIK 

       310        320        330        340        350        360 
VGIGPGSICT TRVVAGVGVP QVTAVMECSK AAREMDRCCI SDGGIKFSGD VVKALAVGAN 

       370        380        390        400        410        420 
TVMVGSLFAG TEESPGETIL YQGRTYKIYR GMGSIDAMKD GSSDRYFQDT NKKLVPEGIV 

       430        440        450        460        470        480 
GRVPYRGPVS DTIYQLVGGL SSGMGYCGAS DLKTLFNTSQ LVIISSAGLR ESHVHDVIIT 

       490 
KEAPNYRVDT P

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References

[1]"The complete genome sequence of Lawsonia intracellularis: the causative agent of proliferative enteropathy."
Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L., Peterson A., May B., Singh S., Gebhart C., Kapur V.
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PHE/MN1-00 EMBL CAJ54645.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM180252 Genomic DNA. Translation: CAJ54645.1.
RefSeqYP_594966.1. NC_008011.1.

3D structure databases

ProteinModelPortalQ1MQT2.
SMRQ1MQT2. Positions 5-487.
ModBaseSearch...

Protein-protein interaction databases

STRING363253.LI0591.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4060257.
KEGGlip:LI0591.
PATRIC22304627. VBILawInt40445_0645.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165755.
KOK00088.
OMASAGLKES.
ProtClustDBCLSK705018.

Enzyme and pathway databases

BioCycLINT363253:GH6E-747-MONOMER.
UniPathwayUPA00601; UER00295.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR000644. Cysta_beta_synth_core.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERPTHR11911:SF6. PTHR11911:SF6. 1 hit.
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 nameQ1MQT2_LAWIP
AccessionPrimary (citable) accession number: Q1MQT2
Entry history
Integrated into UniProtKB/TrEMBL: May 30, 2006
Last sequence update: May 30, 2006
Last modified: May 1, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info