(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BIV6_GEOS0

ID   A0A0F6BIV6_GEOS0        Unreviewed;       257 AA.
AC   A0A0F6BIV6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 20.
DE   RecName: Full=Acid sugar phosphatase {ECO:0000256|PIRNR:PIRNR000915};
DE            EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR000915};
GN   OrderedLocusNames=GY4MC1_0525 {ECO:0000313|EMBL:ADP73357.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73357.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73357.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73357.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the dephosphorylation of 2-6 carbon acid
CC       sugars in vitro. {ECO:0000256|PIRNR:PIRNR000915}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000915};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. NagD
CC       family. {ECO:0000256|PIRNR:PIRNR000915}.
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DR   EMBL; CP002293; ADP73357.1; -; Genomic_DNA.
DR   EnsemblBacteria; ADP73357; ADP73357; GY4MC1_0525.
DR   KEGG; gmc:GY4MC1_0525; -.
DR   KO; K01101; -.
DR   OMA; VFGTAYC; -.
DR   BioCyc; GSP581103:G1GOQ-576-MONOMER; -.
DR   Proteomes; UP000002034; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 2.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006357; HAD-SF_hydro_IIA.
DR   InterPro; IPR006354; HAD-SF_hydro_IIA_hyp1.
DR   InterPro; IPR023214; HAD_sf.
DR   Pfam; PF13344; Hydrolase_6; 1.
DR   PIRSF; PIRSF000915; PGP-type_phosphatase; 2.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
DR   TIGRFAMs; TIGR01457; HAD-SF-IIA-hyp2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BIV6.
DR   SWISS-2DPAGE; A0A0F6BIV6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Hydrolase {ECO:0000313|EMBL:ADP73357.1};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR000915};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000915}.
FT   ACT_SITE     11     11       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR000915-1}.
FT   ACT_SITE     13     13       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000915-1}.
SQ   SEQUENCE   257 AA;  28413 MW;  D18F9D62C5858739 CRC64;
     MLKKYKGYLI DLDGTMYRGT ECIAEARDFV KALYQKGIPY LFVTNNSSRT PAQVAEKLQS
     FGVPATEEHV FTTSQATANY IFEKKPDASI YVIGEEGLRT ALEEKGFAFA KEDAEFVVMG
     IDRNITYEKL AIACLAVRNG ATFISTNADI ALPTERGLLP GNGSLTAVVA VSTQVQPIFI
     GKPEKIIMEQ ALKVLGVPRE ETLMIGDYYD TDIMAGMNAG VDTLLVHTGV TTKELLQRYE
     KQPTYTADSL KEWIDRI
//

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