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P0C0H6

- IMDH_STRPY

UniProt

P0C0H6 - IMDH_STRPY

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Protein
Inosine-5'-monophosphate dehydrogenase
Gene
guaB, impD
Organism
Streptococcus pyogenes
Status
Reviewed - Annotation score: 5 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 By similarity.UniRule annotation

Catalytic activityi

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

Cofactori

Potassium By similarity.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 By similarity.UniRule annotation

Kineticsi

  1. KM=62 µM for Inosine 5'-phosphate1 Publication
  2. KM=1180 µM for NAD+

pH dependencei

Optimum pH is 7.8.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei253 – 2531NAD By similarity
Metal bindingi305 – 3051Potassium; via carbonyl oxygen By similarity
Metal bindingi307 – 3071Potassium; via carbonyl oxygen By similarity
Binding sitei308 – 3081IMP
Active sitei310 – 3101Thioimidate intermediate By similarity
Metal bindingi310 – 3101Potassium; via carbonyl oxygen By similarity
Binding sitei421 – 4211IMP By similarity
Metal bindingi475 – 4751Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi476 – 4761Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi477 – 4771Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi303 – 3053NAD By similarity

GO - Molecular functioni

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

SABIO-RKP0C0H6.
UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenase (EC:1.1.1.205)
Short name:
IMP dehydrogenase
Short name:
IMPD
Short name:
IMPDH
Gene namesi
Name:guaB
Synonyms:impD
OrganismiStreptococcus pyogenes
Taxonomic identifieri1314 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi406 – 4061R → A: No activity. 1 Publication
Mutagenesisi421 – 4211E → Q: No activity. 1 Publication
Mutagenesisi450 – 4501Y → A: No effect. 1 Publication
Mutagenesisi450 – 4501Y → D: Reduces activity by 75%. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 493492Inosine-5'-monophosphate dehydrogenaseUniRule annotation
PRO_0000093714Add
BLAST

Proteomic databases

PRIDEiP0C0H6.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64
Helixi15 – 173
Beta strandi18 – 203
Helixi29 – 313
Beta strandi36 – 394
Beta strandi42 – 509
Turni54 – 563
Helixi59 – 679
Beta strandi71 – 744
Helixi80 – 9314
Turni94 – 974
Beta strandi98 – 1003
Beta strandi106 – 1094
Helixi110 – 11910
Beta strandi123 – 1297
Turni131 – 1333
Beta strandi135 – 1417
Helixi142 – 1476
Beta strandi151 – 1544
Turni155 – 1573
Helixi173 – 18210
Beta strandi186 – 1916
Beta strandi195 – 2028
Helixi203 – 2119
Beta strandi226 – 2294
Helixi235 – 24511
Beta strandi248 – 2525
Helixi260 – 27213
Beta strandi274 – 2763
Beta strandi278 – 2836
Helixi286 – 2949
Beta strandi298 – 3025
Helixi312 – 3154
Helixi322 – 33514
Beta strandi339 – 3446
Helixi349 – 3579
Beta strandi361 – 3666
Turni367 – 3715
Beta strandi372 – 3743
Beta strandi379 – 3824
Beta strandi385 – 3917
Helixi396 – 3994
Beta strandi424 – 4285
Helixi433 – 45018
Helixi456 – 4627
Beta strandi465 – 4673
Helixi470 – 4767

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZFJX-ray1.90A2-492[»]
ProteinModelPortaliP0C0H6.
SMRiP0C0H6. Positions 2-491.

Miscellaneous databases

EvolutionaryTraceiP0C0H6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini97 – 15559CBS 1
Add
BLAST
Domaini159 – 21961CBS 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni343 – 3453IMP bindingUniRule annotation
Regioni366 – 3672IMP bindingUniRule annotation
Regioni390 – 3945IMP bindingUniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.

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]
PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0C0H6-1 [UniParc]FASTAAdd to Basket

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MSNWDTKFLK KGYTFDDVLL IPAESHVLPN EVDLKTKLAD NLTLNIPIIT    50
AAMDTVTGSK MAIAIARAGG LGVIHKNMSI TEQAEEVRKV KRSENGVIID 100
PFFLTPEHKV SEAEELMQRY RISGVPIVET LANRKLVGII TNRDMRFISD 150
YNAPISEHMT SEHLVTAAVG TDLETAERIL HEHRIEKLPL VDNSGRLSGL 200
ITIKDIEKVI EFPHAAKDEF GRLLVAAAVG VTSDTFERAE ALFEAGADAI 250
VIDTAHGHSA GVLRKIAEIR AHFPNRTLIA GNIATAEGAR ALYDAGVDVV 300
KVGIGPGSIC TTRVVAGVGV PQVTAIYDAA AVAREYGKTI IADGGIKYSG 350
DIVKALAAGG NAVMLGSMFA GTDEAPGETE IYQGRKFKTY RGMGSIAAMK 400
KGSSDRYFQG SVNEANKLVP EGIEGRVAYK GAASDIVFQM LGGIRSGMGY 450
VGAGDIQELH ENAQFVEMSG AGLIESHPHD VQITNEAPNY SVH 493
Length:493
Mass (Da):52,807
Last modified:January 23, 2007 - v2
Checksum:i9C317AD598CB5740
GO

Mass spectrometryi

Molecular mass is 52328 Da from positions 2 - 493. Determined by MALDI. 1 Publication

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti419 – 4191V → L no nucleotide entry 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U26056 Genomic DNA. Translation: AAB03846.1.
PIRiJC4372.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U26056 Genomic DNA. Translation: AAB03846.1 .
PIRi JC4372.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZFJ X-ray 1.90 A 2-492 [» ]
ProteinModelPortali P0C0H6.
SMRi P0C0H6. Positions 2-491.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P0C0H6.

Proteomic databases

PRIDEi P0C0H6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0517.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
SABIO-RK P0C0H6.

Miscellaneous databases

EvolutionaryTracei P0C0H6.

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 ]
PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
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

  1. "Cloning, sequence analysis and expression of the group A streptococcal guaB gene encoding inosine monophosphate dehydrogenase."
    Ashbaugh C.D., Wessels M.R.
    Gene 165:57-60(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase."
    Zhang R.G., Evans G., Rotella F.J., Westbrook E.M., Beno D., Huberman E., Joachimiak A., Collart F.R.
    Biochemistry 38:4691-4700(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH IMP, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, SUBUNIT, MUTAGENESIS OF ARG-406; GLU-421 AND TYR-450.

Entry informationi

Entry nameiIMDH_STRPY
AccessioniPrimary (citable) accession number: P0C0H6
Secondary accession number(s): P50099, P68838
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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

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