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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-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)
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 sitei247NADUniRule annotation1
Metal bindingi296Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi298Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei299IMP1
Active sitei301Thioimidate intermediateUniRule annotation1
Metal bindingi301Potassium; via carbonyl oxygenUniRule annotation1
Active sitei397Proton acceptorUniRule annotation1
Binding sitei412IMP1
Metal bindingi466Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi467Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi468Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi294 – 296NADUniRule 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:PH0307
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000937221 – 486Inosine-5'-monophosphate dehydrogenaseAdd BLAST486

Proteomic databases

PRIDEiO58045.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi70601.PH0307.

Structurei

Secondary structure

1486
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 9Combined sources6
Helixi17 – 19Combined sources3
Beta strandi20 – 22Combined sources3
Beta strandi38 – 41Combined sources4
Beta strandi44 – 52Combined sources9
Turni56 – 58Combined sources3
Helixi61 – 69Combined sources9
Beta strandi73 – 76Combined sources4
Beta strandi78 – 80Combined sources3
Helixi82 – 93Combined sources12
Beta strandi222 – 225Combined sources4
Helixi230 – 238Combined sources9
Beta strandi242 – 247Combined sources6
Helixi254 – 265Combined sources12
Beta strandi269 – 276Combined sources8
Helixi279 – 282Combined sources4
Beta strandi288 – 293Combined sources6
Helixi303 – 306Combined sources4
Helixi313 – 326Combined sources14
Beta strandi330 – 335Combined sources6
Helixi340 – 348Combined sources9
Beta strandi352 – 357Combined sources6
Turni358 – 362Combined sources5
Beta strandi370 – 373Combined sources4
Beta strandi376 – 382Combined sources7
Helixi387 – 390Combined sources4
Beta strandi415 – 419Combined sources5
Helixi424 – 441Combined sources18
Helixi447 – 453Combined sources7
Beta strandi456 – 458Combined sources3
Helixi461 – 467Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CU0X-ray2.10A/B1-486[»]
ProteinModelPortaliO58045.
SMRiO58045.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO58045.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini99 – 154CBS 1UniRule annotationAdd BLAST56
Domaini156 – 215CBS 2UniRule annotationAdd BLAST60

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni334 – 336IMP binding3
Regioni357 – 358IMP binding2
Regioni381 – 385IMP binding5

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiarCOG00612. Archaea.
ENOG4102TCX. Archaea.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165755.
KOiK00088.
OMAiSSMGYCG.

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.

O58045-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKFVEKLEK AIKGYTFDDV LLIPQATEVE PKDVDVSTRI TPNVKLNIPI
60 70 80 90 100
LSAAMDTVTE WEMAVAMARE GGLGVIHRNM GIEEQVEQVK RVKRAERLIV
110 120 130 140 150
EDVITIAPDE TVDFALFLME KHGIDGLPVV EDEKVVGIIT KKDIAAREGK
160 170 180 190 200
LVKELMTKEV ITVPESIEVE EALKIMIENR IDRLPVVDER GKLVGLITMS
210 220 230 240 250
DLVARKKYKN AVRDENGELL VAAAVSPFDI KRAIELDKAG VDVIVVDTAH
260 270 280 290 300
AHNLKAIKSM KEMRQKVDAD FIVGNIANPK AVDDLTFADA VKVGIGPGSI
310 320 330 340 350
CTTRIVAGVG VPQITAVAMV ADRAQEYGLY VIADGGIRYS GDIVKAIAAG
360 370 380 390 400
ADAVMLGNLL AGTKEAPGKE VIINGRKYKQ YRGMGSLGAM MKGGAERYYQ
410 420 430 440 450
GGYMKTRKFV PEGVEGVVPY RGTVSEVLYQ LVGGLKAGMG YVGARNIREL
460 470 480
KEKGEFVIIT HAGIKESHPH DIIITNEAPN YPLEKF
Length:486
Mass (Da):52,933
Last modified:August 1, 1998 - v1
Checksum:i6B21E9B7B3AA7C3C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA29380.1.
PIRiE71456.
RefSeqiWP_010884401.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA29380; BAA29380; BAA29380.
GeneIDi1444188.
KEGGipho:PH0307.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA29380.1.
PIRiE71456.
RefSeqiWP_010884401.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CU0X-ray2.10A/B1-486[»]
ProteinModelPortaliO58045.
SMRiO58045.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH0307.

Proteomic databases

PRIDEiO58045.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA29380; BAA29380; BAA29380.
GeneIDi1444188.
KEGGipho:PH0307.

Phylogenomic databases

eggNOGiarCOG00612. Archaea.
ENOG4102TCX. Archaea.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165755.
KOiK00088.
OMAiSSMGYCG.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.

Miscellaneous databases

EvolutionaryTraceiO58045.

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_PYRHO
AccessioniPrimary (citable) accession number: O58045
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 2, 2016
This is version 120 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

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.