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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi53 – 531Zinc; catalytic
Active sitei55 – 551Proton donorBy similarity
Metal bindingi83 – 831Zinc; catalytic
Metal bindingi86 – 861Zinc; catalytic

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 156156Guanine deaminasePRO_0000171704Add
BLAST

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

1
156
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1917Combined sources
Beta strandi22 – 254Combined sources
Beta strandi27 – 326Combined sources
Beta strandi35 – 417Combined sources
Helixi44 – 474Combined sources
Helixi54 – 6613Combined sources
Beta strandi68 – 703Combined sources
Beta strandi75 – 806Combined sources
Helixi84 – 9310Combined sources
Beta strandi96 – 1027Combined sources
Helixi104 – 1096Combined sources
Helixi114 – 1218Combined sources
Helixi125 – 1273Combined sources
Beta strandi128 – 1303Combined sources
Beta strandi132 – 1343Combined sources
Turni138 – 1414Combined sources
Helixi142 – 1498Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO34598.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 132132CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107Y2X. Bacteria.
COG0590. LUCA.
HOGENOMiHOG000085049.
InParanoidiO34598.
KOiK01487.
OMAiFDDQFIY.
OrthoDBiEOG64FKGZ.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1TIYX-ray2.50A/B1-156[»]
1WKQX-ray1.17A/B1-156[»]
ProteinModelPortaliO34598.
SMRiO34598. Positions 1-156.
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.
OMAiFDDQFIY.
OrthoDBiEOG64FKGZ.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the Bacillus subtilis genome between xlyA and ykoR."
    Devine K.M.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Bacillus subtilis guanine deaminase is encoded by the yknA gene and is induced during growth with purines as the nitrogen source."
    Nygaard P., Bested S.M., Andersen K.A.K., Saxild H.H.
    Microbiology 146:3061-3069(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: 168.
  4. "Crystal structure of Bacillus subtilis guanine deaminase: the first domain-swapped structure in the cytidine deaminase superfamily."
    Liaw S.-H., Chang Y.-J., Lai C.-T., Chang H.-C., Chang G.-G.
    J. Biol. Chem. 279:35479-35485(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.17 ANGSTROMS) IN COMPLEX WITH ZINC IONS.
  5. "X-ray structure of guanine deaminase from Bacillus subtilis."
    Northeast structural genomics consortium (NESG)
    Submitted (JAN-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ZINC IONS.

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: February 17, 2016
This is version 104 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.