O34598 (GUAD_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanine deaminase
Short name=GDEase
Short name=Guanase
Short name=Guanine aminase
EC=3.5.4.3

Alternative name(s):
Guanine aminohydrolase
Short name=GAH

Gene names

Name:	guaD
Synonyms:	gde
Ordered Locus Names:	BSU13170

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	156 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia. Ref.3
Catalytic activity	Guanine + H2O = xanthine + NH3.
Cofactor	Zinc By similarity.
Pathway	Purine metabolism; guanine degradation; xanthine from guanine: step 1/1.
Induction	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.
Sequence similarities	Belongs to the cytidine and deoxycytidylate deaminase family.

Ontologies

Keywords
Biological process	Purine metabolism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	purine base metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	guanine deaminase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 156

156

Guanine deaminase

PRO_0000171704

Sites

Active site

55

1

Proton donor By similarity

Metal binding

53

1

Zinc; catalytic

Metal binding

83

1

Zinc; catalytic

Metal binding

86

1

Zinc; catalytic

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

156

Helix Strand Turn

Details...

Helix

3 – 19

17

Beta strand

22 – 25

4

Beta strand

27 – 32

6

Beta strand

35 – 41

7

Helix

44 – 47

4

Helix

54 – 66

13

Beta strand

68 – 70

3

Beta strand

75 – 80

6

Helix

84 – 93

10

Beta strand

96 – 102

7

Helix

104 – 109

6

Helix

114 – 121

8

Helix

125 – 127

3

Beta strand

128 – 130

3

Beta strand

132 – 134

3

Turn

138 – 141

4

Helix

142 – 149

8

Sequences

	Sequence		Length	Mass (Da)
	O34598 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: B6498345A98BC214	FASTA	156	17,156
	10 20 30 40 50 60 MNHETFLKRA VTLACEGVNA GIGGPFGAVI VKDGAIIAEG QNNVTTSNDP TAHAEVTAIR 70 80 90 100 110 120 KACKVLGAYQ LDDCILYTSC EPCPMCLGAI YWARPKAVFY AAEHTDAAEA GFDDSFIYKE 130 140 150 IDKPAEERTI PFYQVTLTEH LSPFQAWRNF ANKKEY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9384377] [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: 11101664] [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: 15180998] [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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ002571 Genomic DNA. Translation: CAA05596.1.
AL009126 Genomic DNA. Translation: CAB13174.1.

PIR

F69857.

RefSeq

NP_389200.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TIY	X-ray	2.50	A/B	1-156	[»]
1WKQ	X-ray	1.17	A/B	1-156	[»]

ProteinModelPortal

O34598.

SMR

O34598. Positions 1-156.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000000911; EBBACP00000000911; EBBACG00000000909.

GeneID

936695.

GenomeReviews

Gene locus BSU13170 in contig AL009126_GR.

KEGG

bsu:BSU13170.

NMPDR

fig|224308.1.peg.1319.

PATRIC

18974393. VBIBacSub10457_1389.

Organism-specific databases

GenoList

BSU13170. [Micado]

Phylogenomic databases

GeneTree

EBGT00050000002012.

HOGENOM

HBG741046.

OMA

HNTVVGD.

PhylomeDB

O34598.

ProtClustDB

CLSK887168.

Enzyme and pathway databases

BioCyc

BSUB:BSU13170-MONOMER.

Family and domain databases

InterPro

IPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
[Graphical view]

KO

K01487.

Pfam

PF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]

SUPFAM

SSF53927. Cytidine_deaminase-like. 1 hit.

PROSITE

PS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GUAD_BACSU

Accession

Primary (citable) accession number: O34598

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program