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O58045

- IMDH_PYRHO

UniProt

O58045 - IMDH_PYRHO

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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: 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

Potassium.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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei247 – 2471NADUniRule annotation
Metal bindingi296 – 2961Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi298 – 2981Potassium; via carbonyl oxygenUniRule annotation
Binding sitei299 – 2991IMP
Active sitei301 – 3011Thioimidate intermediateUniRule annotation
Metal bindingi301 – 3011Potassium; via carbonyl oxygenUniRule annotation
Binding sitei412 – 4121IMP
Metal bindingi466 – 4661Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi467 – 4671Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi468 – 4681Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi294 – 2963NADUniRule annotation

GO - Molecular functioni

  1. adenyl nucleotide binding Source: InterPro
  2. IMP dehydrogenase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. GMP biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Potassium

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-289-MONOMER.
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
ProteomesiUP000000752: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Inosine-5'-monophosphate dehydrogenasePRO_0000093722Add
BLAST

Proteomic databases

PRIDEiO58045.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi70601.PH0307.

Structurei

Secondary structure

1
486
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 96
Helixi17 – 193
Beta strandi20 – 223
Beta strandi38 – 414
Beta strandi44 – 529
Turni56 – 583
Helixi61 – 699
Beta strandi73 – 764
Beta strandi78 – 803
Helixi82 – 9312
Beta strandi222 – 2254
Helixi230 – 2389
Beta strandi242 – 2476
Helixi254 – 26512
Beta strandi269 – 2768
Helixi279 – 2824
Beta strandi288 – 2936
Helixi303 – 3064
Helixi313 – 32614
Beta strandi330 – 3356
Helixi340 – 3489
Beta strandi352 – 3576
Turni358 – 3625
Beta strandi370 – 3734
Beta strandi376 – 3827
Helixi387 – 3904
Beta strandi415 – 4195
Helixi424 – 44118
Helixi447 – 4537
Beta strandi456 – 4583
Helixi461 – 4677

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CU0X-ray2.10A/B1-486[»]
ProteinModelPortaliO58045.
SMRiO58045. Positions 3-480.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO58045.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini99 – 15456CBS 1UniRule annotationAdd
BLAST
Domaini156 – 21560CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni334 – 3363IMP binding
Regioni357 – 3582IMP binding
Regioni381 – 3855IMP binding

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
HOGENOMiHOG000165755.
KOiK00088.
OMAiYEALTFD.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
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:
EMBL
GenBank
DDBJ
Links Updated
BA000001 Genomic DNA. Translation: BAA29380.1.
PIRiE71456.
RefSeqiNP_142293.1. NC_000961.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000001 Genomic DNA. Translation: BAA29380.1 .
PIRi E71456.
RefSeqi NP_142293.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CU0 X-ray 2.10 A/B 1-486 [» ]
ProteinModelPortali O58045.
SMRi O58045. Positions 3-480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 70601.PH0307.

Proteomic databases

PRIDEi O58045.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAA29380 ; BAA29380 ; BAA29380 .
GeneIDi 1444188.
KEGGi pho:PH0307.

Phylogenomic databases

eggNOGi COG0517.
HOGENOMi HOG000165755.
KOi K00088.
OMAi YEALTFD.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
BioCyci PHOR70601:GJWR-289-MONOMER.

Miscellaneous databases

EvolutionaryTracei O58045.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01964. IMPDH.
InterProi IPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view ]
Pfami PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000130. IMPDH. 1 hit.
SMARTi SM00116. CBS. 2 hits.
[Graphical view ]
TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
PROSITEi PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  2. "Crystal structure of inosine-5'-monophosphate dehydrogenase from Pyrococcus horikoshii OT3."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUL-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH XMP.
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

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: October 1, 2014
This is version 107 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

External Data

Dasty 3