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Protein

Guanine deaminase

Gene

guaD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.1 Publication

Catalytic activityi

Guanine + H2O = xanthine + NH3.

Cofactori

Zn2+By similarity

Pathwayi: guanine degradation

This protein is involved in step 1 of the subpathway that synthesizes xanthine from guanine.
Proteins known to be involved in this subpathway in this organism are:
  1. Guanine deaminase (guaD)
This subpathway is part of the pathway guanine degradation, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes xanthine from guanine, the pathway guanine degradation and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi53Zinc; catalytic1
Active sitei55Proton donorBy similarity1
Metal bindingi83Zinc; catalytic1
Metal bindingi86Zinc; catalytic1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Purine metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU13170-MONOMER.
BRENDAi3.5.4.3. 658.
UniPathwayiUPA00603; UER00660.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine deaminase (EC:3.5.4.3)
Short name:
GDEase
Short name:
Guanase
Short name:
Guanine aminase
Alternative name(s):
Guanine aminohydrolase
Short name:
GAH
Gene namesi
Name:guaD
Synonyms:gde
Ordered Locus Names:BSU13170
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001717041 – 156Guanine deaminaseAdd BLAST156

Proteomic databases

PaxDbiO34598.

Expressioni

Inductioni

Expressed only during limited or partially limited nitrogen conditions. Can be induced to high levels in the presence of purines or intermediates of the purine catabolic pathway. Expression seems indirectly controlled by TnrA and GlnR.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100007296.

Structurei

Secondary structure

1156
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 19Combined sources17
Beta strandi22 – 25Combined sources4
Beta strandi27 – 32Combined sources6
Beta strandi35 – 41Combined sources7
Helixi44 – 47Combined sources4
Helixi54 – 66Combined sources13
Beta strandi68 – 70Combined sources3
Beta strandi75 – 80Combined sources6
Helixi84 – 93Combined sources10
Beta strandi96 – 102Combined sources7
Helixi104 – 109Combined sources6
Helixi114 – 121Combined sources8
Helixi125 – 127Combined sources3
Beta strandi128 – 130Combined sources3
Beta strandi132 – 134Combined sources3
Turni138 – 141Combined sources4
Helixi142 – 149Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TIYX-ray2.50A/B1-156[»]
1WKQX-ray1.17A/B1-156[»]
ProteinModelPortaliO34598.
SMRiO34598.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34598.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 132CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd BLAST132

Sequence similaritiesi

Contains 1 CMP/dCMP-type deaminase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4107Y2X. Bacteria.
COG0590. LUCA.
HOGENOMiHOG000085049.
InParanoidiO34598.
KOiK01487.
OMAiLSGCEIY.
PhylomeDBiO34598.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O34598-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNHETFLKRA VTLACEGVNA GIGGPFGAVI VKDGAIIAEG QNNVTTSNDP
60 70 80 90 100
TAHAEVTAIR KACKVLGAYQ LDDCILYTSC EPCPMCLGAI YWARPKAVFY
110 120 130 140 150
AAEHTDAAEA GFDDSFIYKE IDKPAEERTI PFYQVTLTEH LSPFQAWRNF

ANKKEY
Length:156
Mass (Da):17,156
Last modified:January 1, 1998 - v1
Checksum:iB6498345A98BC214
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002571 Genomic DNA. Translation: CAA05596.1.
AL009126 Genomic DNA. Translation: CAB13174.1.
PIRiF69857.
RefSeqiNP_389200.1. NC_000964.3.
WP_003245084.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13174; CAB13174; BSU13170.
GeneIDi936695.
KEGGibsu:BSU13170.
PATRICi18974393. VBIBacSub10457_1389.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002571 Genomic DNA. Translation: CAA05596.1.
AL009126 Genomic DNA. Translation: CAB13174.1.
PIRiF69857.
RefSeqiNP_389200.1. NC_000964.3.
WP_003245084.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TIYX-ray2.50A/B1-156[»]
1WKQX-ray1.17A/B1-156[»]
ProteinModelPortaliO34598.
SMRiO34598.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100007296.

Proteomic databases

PaxDbiO34598.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13174; CAB13174; BSU13170.
GeneIDi936695.
KEGGibsu:BSU13170.
PATRICi18974393. VBIBacSub10457_1389.

Phylogenomic databases

eggNOGiENOG4107Y2X. Bacteria.
COG0590. LUCA.
HOGENOMiHOG000085049.
InParanoidiO34598.
KOiK01487.
OMAiLSGCEIY.
PhylomeDBiO34598.

Enzyme and pathway databases

UniPathwayiUPA00603; UER00660.
BioCyciBSUB:BSU13170-MONOMER.
BRENDAi3.5.4.3. 658.

Miscellaneous databases

EvolutionaryTraceiO34598.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUAD_BACSU
AccessioniPrimary (citable) accession number: O34598
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: January 1, 1998
Last modified: November 2, 2016
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, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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.