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P0C0H6

- IMDH_STRPY

UniProt

P0C0H6 - IMDH_STRPY

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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

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.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

Kineticsi

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

pH dependencei

Optimum pH is 7.8.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei253 – 2531NADUniRule annotation
Metal bindingi305 – 3051Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi307 – 3071Potassium; via carbonyl oxygenUniRule annotation
Binding sitei308 – 3081IMP1 PublicationUniRule annotation
Active sitei310 – 3101Thioimidate intermediateUniRule annotation
Metal bindingi310 – 3101Potassium; via carbonyl oxygenUniRule annotation
Binding sitei421 – 4211IMPUniRule annotation
Metal bindingi475 – 4751Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi476 – 4761Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi477 – 4771Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi303 – 3053NADUniRule 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

SABIO-RKP0C0H6.
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
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 dehydrogenasePRO_0000093714Add
BLAST

Proteomic databases

PRIDEiP0C0H6.

Interactioni

Subunit structurei

Homotetramer.1 PublicationUniRule annotation

Structurei

Secondary structure

1
493
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64Combined sources
Helixi15 – 173Combined sources
Beta strandi18 – 203Combined sources
Helixi29 – 313Combined sources
Beta strandi36 – 394Combined sources
Beta strandi42 – 509Combined sources
Turni54 – 563Combined sources
Helixi59 – 679Combined sources
Beta strandi71 – 744Combined sources
Helixi80 – 9314Combined sources
Turni94 – 974Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi106 – 1094Combined sources
Helixi110 – 11910Combined sources
Beta strandi123 – 1297Combined sources
Turni131 – 1333Combined sources
Beta strandi135 – 1417Combined sources
Helixi142 – 1476Combined sources
Beta strandi151 – 1544Combined sources
Turni155 – 1573Combined sources
Helixi173 – 18210Combined sources
Beta strandi186 – 1916Combined sources
Beta strandi195 – 2028Combined sources
Helixi203 – 2119Combined sources
Beta strandi226 – 2294Combined sources
Helixi235 – 24511Combined sources
Beta strandi248 – 2525Combined sources
Helixi260 – 27213Combined sources
Beta strandi274 – 2763Combined sources
Beta strandi278 – 2836Combined sources
Helixi286 – 2949Combined sources
Beta strandi298 – 3025Combined sources
Helixi312 – 3154Combined sources
Helixi322 – 33514Combined sources
Beta strandi339 – 3446Combined sources
Helixi349 – 3579Combined sources
Beta strandi361 – 3666Combined sources
Turni367 – 3715Combined sources
Beta strandi372 – 3743Combined sources
Beta strandi379 – 3824Combined sources
Beta strandi385 – 3917Combined sources
Helixi396 – 3994Combined sources
Beta strandi424 – 4285Combined sources
Helixi433 – 45018Combined sources
Helixi456 – 4627Combined sources
Beta strandi465 – 4673Combined sources
Helixi470 – 4767Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZFJX-ray1.90A2-492[»]
ProteinModelPortaliP0C0H6.
SMRiP0C0H6. Positions 2-491.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0H6.

Family & Domainsi

Domains and Repeats

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

Region

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

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

« Hide

        10         20         30         40         50
MSNWDTKFLK KGYTFDDVLL IPAESHVLPN EVDLKTKLAD NLTLNIPIIT
60 70 80 90 100
AAMDTVTGSK MAIAIARAGG LGVIHKNMSI TEQAEEVRKV KRSENGVIID
110 120 130 140 150
PFFLTPEHKV SEAEELMQRY RISGVPIVET LANRKLVGII TNRDMRFISD
160 170 180 190 200
YNAPISEHMT SEHLVTAAVG TDLETAERIL HEHRIEKLPL VDNSGRLSGL
210 220 230 240 250
ITIKDIEKVI EFPHAAKDEF GRLLVAAAVG VTSDTFERAE ALFEAGADAI
260 270 280 290 300
VIDTAHGHSA GVLRKIAEIR AHFPNRTLIA GNIATAEGAR ALYDAGVDVV
310 320 330 340 350
KVGIGPGSIC TTRVVAGVGV PQVTAIYDAA AVAREYGKTI IADGGIKYSG
360 370 380 390 400
DIVKALAAGG NAVMLGSMFA GTDEAPGETE IYQGRKFKTY RGMGSIAAMK
410 420 430 440 450
KGSSDRYFQG SVNEANKLVP EGIEGRVAYK GAASDIVFQM LGGIRSGMGY
460 470 480 490
VGAGDIQELH ENAQFVEMSG AGLIESHPHD VQITNEAPNY SVH
Length:493
Mass (Da):52,807
Last modified:January 23, 2007 - v2
Checksum:i9C317AD598CB5740
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti419 – 4191V → L no nucleotide entry (PubMed:10200156)Curated

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26056 Genomic DNA. Translation: AAB03846.1.
PIRiJC4372.
RefSeqiWP_002991454.1. NZ_JHTQ01000034.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26056 Genomic DNA. Translation: AAB03846.1 .
PIRi JC4372.
RefSeqi WP_002991454.1. NZ_JHTQ01000034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 60 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