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P44334 (IMDH_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Inosine-5'-monophosphate dehydrogenase
Short name=IMP dehydrogenase
Short name=IMPD
Short name=IMPDH
EC=1.1.1.205
Gene names
Name:guaB
Ordered Locus Names:HI_0221
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus ›

Protein attributes

Sequence length488 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. HAMAP-Rule MF_01964

Cofactor

Potassium By similarity.

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. HAMAP-Rule MF_01964

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093697

Regions

Domain94 – 15057CBS 1
Domain154 – 21562CBS 2
Nucleotide binding249 – 2513NAD By similarity
Nucleotide binding299 – 3013NAD By similarity
Region339 – 3413IMP binding By similarity
Region362 – 3632IMP binding By similarity
Region386 – 3905IMP binding By similarity

Sites

Active site3061Thioimidate intermediate By similarity
Metal binding3011Potassium; via carbonyl oxygen By similarity
Metal binding3031Potassium; via carbonyl oxygen By similarity
Metal binding3061Potassium; via carbonyl oxygen By similarity
Metal binding4701Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4711Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4721Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2491NAD By similarity
Binding site3041IMP By similarity
Binding site4161IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
P44334 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: B477F22344E4BE8B

FASTA48851,981
        10         20         30         40         50         60 
MSLRIKQEAL TFDDVLLVPA HSTVLPNTAN LSTQLTKEIR LNIPMLSAAM DTVTETKLAI 

        70         80         90        100        110        120 
SLAQEGGIGF IHKNMTIERQ ADRVRKVKKF ESGIVSEPVT VLPNLTLAEL AEMVKKNGFA 

       130        140        150        160        170        180 
GYPVVDGENN LIGIITGRDT RFVKDLSKTV SQVMTKKEDL VTVKEGASRE EILELMHQHR 

       190        200        210        220        230        240 
VEKVLVVNDS FKLKGMITVK DFQKAEQKPN ACKDEFGRLR VGAAVGAGAG NEERIDALVK 

       250        260        270        280        290        300 
AGVDVLLIDS SHGHSEGVLQ RVRETRAKYP NLPIVAGNVA TAEGAIALAD AGASAVKVGI 

       310        320        330        340        350        360 
GPGSICTTRI VTGVGVPQIT AIADAAAALK DRGIPVIADG GIRFSGDIAK AIAAGASCVM 

       370        380        390        400        410        420 
VGSMFAGTEE APGEIELYQG RAFKSYRGMG SLGAMAKGSS DRYFQSDNAA DKLVPEGIEG 

       430        440        450        460        470        480 
RIPYKGYLKE IIHQQMGGLR SCMGLTGCAT IDELRTKAEF VRISGAGIKE SHVHDVAITK 


EAPNYRMG

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42023 Genomic DNA. Translation: AAC21890.1.
PIRH64055.
RefSeqNP_438392.1. NC_000907.1.

3D structure databases

ProteinModelPortalP44334.
SMRP44334. Positions 3-486.
ModBaseSearch...

Protein-protein interaction databases

STRING71421.HI0221.

Proteomic databases

PRIDEP44334.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC21890; AAC21890; HI_0221.
GeneID951137.
KEGGhin:HI0221.
PATRIC20188961. VBIHaeInf48452_0233.

Phylogenomic databases

eggNOGCOG0517.
KOK00088.
OMASAGLKES.
ProtClustDBPRK05567.

Enzyme and pathway databases

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 nameIMDH_HAEIN
AccessionPrimary (citable) accession number: P44334
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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