Reviewed, UniProtKB/Swiss-Prot O14057 (GUAD_SCHPO)

Names and origin

Protein names

Recommended name:
    Probable guanine deaminase
      Short name=Guanase
      Short name=Guanine aminase
    EC=3.5.4.3
Alternative name(s):
    Guanine aminohydrolase
      Short name=GAH

Gene names

ORF Names:

SPCC1672.03c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	527 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia By similarity.
Catalytic activity	Guanine + H2O = xanthine + NH3.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Pathway	Purine metabolism; guanine degradation; xanthine from guanine: step 1/1.
Sequence similarities	Belongs to the ATZ/TRZ family.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	guanine deaminase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 527	527	Probable guanine deaminase		PRO_0000122301
Sites
	Metal binding	79	1	Zinc; via tele nitrogen By similarity
	Metal binding	81	1	Zinc; via tele nitrogen By similarity
	Metal binding	239	1	Zinc; via tele nitrogen By similarity
	Metal binding	329	1	Zinc By similarity
	Binding site	84	1	Substrate By similarity
	Binding site	212	1	Substrate By similarity
	Binding site	242	1	Substrate By similarity
	Binding site	278	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O14057-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 23D9A3F1117601C1	FASTA	527	58,047
	10 20 30 40 50 60 MDGHTCDVFV GKLIHTPSLG ELEITDATVG VYNGKIVFLE KSMTPKTLEE AKSHHLLKEA 70 80 90 100 110 120 TIHKLKPLQF MFPGLIDTHI HAPQYPNSGI GIDVPLLQWL EKYTFPLESS LADLEEARQV 130 140 150 160 170 180 YKRVVERTLS NGTTFASYFS TLHTPTSALL AEICYSYGQR AYIGKCNMNN LSPDHYCEKS 190 200 210 220 230 240 AESSLEATRQ LISYMSILDP KREMVTPIIT PRFAPSCTED LLSGCGELAE KHNLPIQTHI 250 260 270 280 290 300 SENTSEIELV KELFPERKSY ADVYDYYKLL TPQTILAHAI HLEDEEIELL TKRSSGISHC 310 320 330 340 350 360 PTSNSILASG LANVRKLLDS GINVGLGTDV SGGYAPSILI ALRHAAMTSR SLSYVLGDPK 370 380 390 400 410 420 VMLDLSELLY LATQGGAEVV SRGDQVGSFA VGKYWDALIV DLSAETHSCV DIFERDTWPV 430 440 450 460 470 480 MLSKWVFTSD DRNLAQVWVN GRLVSGFEMK ANLKNSTPLT NGVTSSGHQV FKELTQAHLL 490 500 510 520 PRTQCVDTPP SCCGGHCCKE ESCRTENCKG AYPANATVTV EEDSGMS

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329672 Genomic DNA. Translation: CAA20441.1.
PIR	T41047.
RefSeq	NP_587874.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2539231.
KEGG	spo:SPCC1672.03c.
NMPDR	fig|4896.1.peg.212.
Organism-specific databases
GeneDB_Spombe	SPCC1672.03c.
Phylogenomic databases
OMA	O14057. SESDWEH.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002219-MON.
BRENDA	3.5.4.3. 653.
Gene expression databases
ArrayExpress	O14057.
Family and domain databases
InterPro	IPR006680. Amidohydro_1. IPR014311. Guanine_deaminase. [Graphical view]
PANTHER	PTHR11271:SF6. Guanine_deaminase. 1 hit.
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
TIGRFAMs	TIGR02967. guan_deamin. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GUAD_SCHPO

Accession

Primary (citable) accession number: O14057

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)