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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Bacillus anthracis
Status
Unreviewed-Annotation score: Annotation score: 3 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), 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 sitei251NADUniRule annotation1
Metal bindingi303Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi305Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei306IMPUniRule annotation1
Active sitei308Thioimidate intermediateUniRule annotation1
Metal bindingi308Potassium; via carbonyl oxygenUniRule annotation1
Active sitei404Proton acceptorUniRule annotation1
Binding sitei416IMPUniRule annotation1
Metal bindingi470Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi471Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi472Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi251 – 253NADUniRule annotation3
Nucleotide bindingi301 – 303NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationImported

Keywords - Biological processi

GMP biosynthesisUniRule annotation, Purine biosynthesis

Keywords - Ligandi

Metal-bindingUniRule annotation, NADUniRule annotation, PotassiumUniRule annotation

Enzyme and pathway databases

BioCyciANTHRA:GUAB-MONOMER.
BRENDAi1.1.1.205. 634.
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 annotationImported
Ordered Locus Names:GBAA_0008Imported
ORF Names:A8C77_00065Imported, ABW01_29210Imported
OrganismiBacillus anthracisImported
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome
  • UP000077577 Componenti: Chromosome
  • UP000035904 Componenti: Unassembled WGS sequence

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3329078.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi198094.BA_0008.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TSBX-ray2.60A/B1-487[»]
3TSDX-ray2.65A/B1-487[»]
3USBX-ray2.38A/B1-487[»]
4MJMX-ray2.25A/B/C/D1-94[»]
A/B/C/D201-487[»]
4MY1X-ray2.60A/B/C/D/E/F/G/H1-91[»]
A/B/C/D/E/F/G/H221-487[»]
4MY8X-ray2.29A/B/C/D1-91[»]
A/B/C/D221-487[»]
4MY9X-ray2.59A/B/C/D/E/F/G/H1-91[»]
A/B/C/D/E/F/G/H221-487[»]
4MYAX-ray1.90A/B1-91[»]
A/B221-487[»]
4MYXX-ray2.70A/B/C/D/E/F/G/H1-91[»]
A/B/C/D/E/F/G/H221-487[»]
4QM1X-ray2.80A/B/C/D1-91[»]
A/B/C/D221-487[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini95 – 153CBSInterPro annotationAdd BLAST59
Domaini157 – 215CBSInterPro annotationAdd BLAST59

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni341 – 343IMP bindingUniRule annotation3
Regioni364 – 365IMP bindingUniRule annotation2
Regioni388 – 392IMP bindingUniRule annotation5

Sequence similaritiesi

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

Keywords - Domaini

CBS domainUniRule annotation, RepeatUniRule annotation

Phylogenomic databases

eggNOGiENOG4105CP4. Bacteria.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165754.
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.

Q81W29-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWESKFVKEG LTFDDVLLVP AKSDVLPREV SVKTVLSESL QLNIPLISAG
60 70 80 90 100
MDTVTEADMA IAMARQGGLG IIHKNMSIEQ QAEQVDKVKR SESGVISDPF
110 120 130 140 150
FLTPEHQVYD AEHLMGKYRI SGVPVVNNLD ERKLVGIITN RDMRFIQDYS
160 170 180 190 200
IKISDVMTKE QLITAPVGTT LSEAEKILQK YKIEKLPLVD NNGVLQGLIT
210 220 230 240 250
IKDIEKVIEF PNSAKDKQGR LLVGAAVGVT ADAMTRIDAL VKASVDAIVL
260 270 280 290 300
DTAHGHSQGV IDKVKEVRAK YPSLNIIAGN VATAEATKAL IEAGANVVKV
310 320 330 340 350
GIGPGSICTT RVVAGVGVPQ LTAVYDCATE ARKHGIPVIA DGGIKYSGDM
360 370 380 390 400
VKALAAGAHV VMLGSMFAGV AESPGETEIY QGRQFKVYRG MGSVGAMEKG
410 420 430 440 450
SKDRYFQEGN KKLVPEGIEG RVPYKGPLAD TVHQLVGGLR AGMGYCGAQD
460 470 480
LEFLRENAQF IRMSGAGLLE SHPHHVQITK EAPNYSL
Length:487
Mass (Da):52,374
Last modified:June 1, 2003 - v1
Checksum:iB37C2C27F7C99279
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017334 Genomic DNA. Translation: AAT29088.1.
CP015779 Genomic DNA. Translation: ANH84443.1.
LDPG01000042 Genomic DNA. Translation: KLV14027.1.
RefSeqiWP_000264082.1. NZ_LHUO01000012.1.

Genome annotation databases

EnsemblBacteriaiAAT29088; AAT29088; GBAA_0008.
AJH90646; AJH90646; BF27_2004.
KLV14027; KLV14027; ABW01_29210.
KOM63084; KOM63084; AB168_06335.
KOM67659; KOM67659; AB166_11280.
KOM75107; KOM75107; AB165_01610.
KOM77539; KOM77539; AB167_18060.
KOM85096; KOM85096; AB164_07585.
KOM93707; KOM93707; AB169_08740.
KON07909; KON07909; AB170_00090.
KON16749; KON16749; AB171_19425.
KON25349; KON25349; AB163_03605.
KOR63893; KOR63893; ADT21_00085.
KOR67243; KOR67243; ADT20_14595.
KEGGibanh:HYU01_00070.
bar:GBAA_0008.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017334 Genomic DNA. Translation: AAT29088.1.
CP015779 Genomic DNA. Translation: ANH84443.1.
LDPG01000042 Genomic DNA. Translation: KLV14027.1.
RefSeqiWP_000264082.1. NZ_LHUO01000012.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TSBX-ray2.60A/B1-487[»]
3TSDX-ray2.65A/B1-487[»]
3USBX-ray2.38A/B1-487[»]
4MJMX-ray2.25A/B/C/D1-94[»]
A/B/C/D201-487[»]
4MY1X-ray2.60A/B/C/D/E/F/G/H1-91[»]
A/B/C/D/E/F/G/H221-487[»]
4MY8X-ray2.29A/B/C/D1-91[»]
A/B/C/D221-487[»]
4MY9X-ray2.59A/B/C/D/E/F/G/H1-91[»]
A/B/C/D/E/F/G/H221-487[»]
4MYAX-ray1.90A/B1-91[»]
A/B221-487[»]
4MYXX-ray2.70A/B/C/D/E/F/G/H1-91[»]
A/B/C/D/E/F/G/H221-487[»]
4QM1X-ray2.80A/B/C/D1-91[»]
A/B/C/D221-487[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198094.BA_0008.

Chemistry databases

ChEMBLiCHEMBL3329078.

Protocols and materials databases

DNASUi1083772.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT29088; AAT29088; GBAA_0008.
AJH90646; AJH90646; BF27_2004.
KLV14027; KLV14027; ABW01_29210.
KOM63084; KOM63084; AB168_06335.
KOM67659; KOM67659; AB166_11280.
KOM75107; KOM75107; AB165_01610.
KOM77539; KOM77539; AB167_18060.
KOM85096; KOM85096; AB164_07585.
KOM93707; KOM93707; AB169_08740.
KON07909; KON07909; AB170_00090.
KON16749; KON16749; AB171_19425.
KON25349; KON25349; AB163_03605.
KOR63893; KOR63893; ADT21_00085.
KOR67243; KOR67243; ADT20_14595.
KEGGibanh:HYU01_00070.
bar:GBAA_0008.

Phylogenomic databases

eggNOGiENOG4105CP4. Bacteria.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165754.
KOiK00088.
OMAiSSMGYCG.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.
BioCyciANTHRA:GUAB-MONOMER.
BRENDAi1.1.1.205. 634.

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 nameiQ81W29_BACAN
AccessioniPrimary (citable) accession number: Q81W29
Secondary accession number(s): E9QUK9
, E9QUL0, Q6I531, Q6KYS5
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.