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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

Catalytic activityi

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.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 (ADK18_00010), 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi303 – 3031Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi305 – 3051Potassium; via carbonyl oxygenUniRule annotation
Binding sitei306 – 3061IMPUniRule annotation
Active sitei308 – 3081Thioimidate intermediateUniRule annotation
Metal bindingi308 – 3081Potassium; via carbonyl oxygenUniRule annotation
Active sitei404 – 4041Proton acceptorUniRule annotation
Binding sitei416 – 4161IMPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi251 – 2533NADUniRule annotation
Nucleotide bindingi301 – 3033NADUniRule annotation

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.
BANT260799:GJAJ-13-MONOMER.
BANT261594:GJ7F-13-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)
Gene namesi
Name:guaBImported
Ordered Locus Names:GBAA_0008Imported
ORF Names:ABW01_29210Imported
OrganismiBacillus anthracisImported
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome
  • UP000035904 Componenti: Unassembled WGS sequence

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3329078.

Interactioni

Protein-protein interaction databases

STRINGi198094.BA_0008.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 15359CBSInterPro annotationAdd
BLAST
Domaini157 – 21559CBSInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni341 – 3433IMP bindingUniRule annotation
Regioni364 – 3652IMP bindingUniRule annotation
Regioni388 – 3925IMP bindingUniRule annotation

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CP4. Bacteria.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165754.
KOiK00088.
OMAiSSMGYCG.
OrthoDBiEOG6GTZPV.

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. 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.
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.
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
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

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.
OrthoDBiEOG6GTZPV.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.
BioCyciANTHRA:GUAB-MONOMER.
BANT260799:GJAJ-13-MONOMER.
BANT261594:GJ7F-13-MONOMER.
BRENDAi1.1.1.205. 634.

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. 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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames ancestorImported and Ames AncestorImported.
  2. "Bacillus anthracis inosine 5'-monophosphate dehydrogenase in action: the first bacterial series of structures of phosphate ion-, substrate-, and product-bound complexes."
    Makowska-Grzyska M., Kim Y., Wu R., Wilton R., Gollapalli D.R., Wang X.K., Zhang R., Jedrzejczak R., Mack J.C., Maltseva N., Mulligan R., Binkowski T.A., Gornicki P., Kuhn M.L., Anderson W.F., Hedstrom L., Joachimiak A.
    Biochemistry 51:6148-6163(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS).
  3. "Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase with an Internal Deletion of the CBS Domain from Bacillus anthracis str. Ames complexed with inhibitor A110."
    Kim Y., Makowska-Grzyska M., Gu M., Anderson W.F., Joachimiak A.
    Submitted (SEP-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-91 AND 221-487.
  4. "Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase with an Internal Deletion of the CBS Domain from Bacillus anthracis str. Ames complexed with inhibitor C91."
    Kim Y., Makowska-Grzyska M., Gu M., Anderson W.F., Joachimiak A.
    Submitted (SEP-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-91 AND 221-487.
  5. "Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase with an Internal Deletion of the CBS Domain from Bacillus anthracis str. Ames complexed with inhibitor Q21."
    Kim Y., Makowska-Grzyska M., Gu M., Gorla S.K., Kavitha M., Cuny G., Hedstrom L., Anderson W.F., Joachimiak A.
    Submitted (SEP-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-91 AND 221-487.
  6. "Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase, with a Internal Deletion of CBS Domain from Bacillus anthracis str. Ame complexed with P32."
    Kim Y., Makowska-Grzyska M., Gu M., Anderson W.F., Joachimiak A.
    Submitted (SEP-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-91 AND 221-487.
  7. "Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase, with a Internal Deletion of CBS Domain from Bacillus anthracis str. Ames complexed with P68."
    Kim Y., Makowska-Grzyska M., Gu M., Anderson W.F., Joachimiak A., CSGID
    Submitted (SEP-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-91 AND 221-487.
  8. "Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase, with a Short Internal Deletion of CBS Domain from Bacillus anthracis str. Ames."
    Kim Y., Makowska-Grzyska M., Gu M., Anderson W.F., Joachimiak A.
    Submitted (SEP-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-94 AND 201-487.
  9. "Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase with an Internal Deletion of the CBS Domain from Bacillus anthracis str. Ames complexed with inhibitor D67."
    Kim Y., Makowska-Grzyska M., Gu M., Mandapati K., Gollapalli D., Gorla S.K., Zhang M., Hedstrom L., Anderson W.F., Joachimiak A., CSGID
    Submitted (JUN-2014) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-91 AND 221-487.
  10. "Whole genome sequence and identification of bacterial endophytes from Costus igneus."
    Lee Y.P., Gan H.M., Eng W., Wheatley M.S., Caraballo A., Polter S., Savka M.A., Hudson A.O.
    Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RIT375Imported.

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: May 11, 2016
This is version 125 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.