(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BI04_GEOS0

ID   A0A0F6BI04_GEOS0        Unreviewed;       409 AA.
AC   A0A0F6BI04;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 23.
DE   SubName: Full=Amidase, hydantoinase/carbamoylase family {ECO:0000313|EMBL:ADP73055.1};
DE            EC=3.5.1.87 {ECO:0000313|EMBL:ADP73055.1};
GN   OrderedLocusNames=GY4MC1_0205 {ECO:0000313|EMBL:ADP73055.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73055.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73055.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73055.1,
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.
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DR   EMBL; CP002293; ADP73055.1; -; Genomic_DNA.
DR   RefSeq; WP_013399864.1; NC_014650.1.
DR   EnsemblBacteria; ADP73055; ADP73055; GY4MC1_0205.
DR   KEGG; gmc:GY4MC1_0205; -.
DR   KO; K02083; -.
DR   OMA; IWPHGRW; -.
DR   OrthoDB; 829830at2; -.
DR   BioCyc; GSP581103:G1GOQ-247-MONOMER; -.
DR   Proteomes; UP000002034; Chromosome.
DR   GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050538; F:N-carbamoyl-L-amino-acid hydrolase activity; IEA:UniProtKB-EC.
DR   CDD; cd03884; M20_bAS; 1.
DR   InterPro; IPR010158; Amidase_Cbmase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR32494; PTHR32494; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01879; hydantase; 1.
PE   4: Predicted;
DR   PRODOM; A0A0F6BI04.
DR   SWISS-2DPAGE; A0A0F6BI04.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Hydrolase {ECO:0000313|EMBL:ADP73055.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   DOMAIN      208    309       M20_dimer. {ECO:0000259|Pfam:PF07687}.
FT   METAL        79     79       Zinc 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   METAL        90     90       Zinc 1. {ECO:0000256|PIRSR:PIRSR001235-
FT                                1}.
FT   METAL        90     90       Zinc 2. {ECO:0000256|PIRSR:PIRSR001235-
FT                                1}.
FT   METAL       125    125       Zinc 2. {ECO:0000256|PIRSR:PIRSR001235-
FT                                1}.
FT   METAL       189    189       Zinc 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   METAL       380    380       Zinc 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001235-1}.
SQ   SEQUENCE   409 AA;  43726 MW;  8F5AA1155522159B CRC64;
     MINGDRLWNR LLELGTIGKQ PSGGITRLSF TKEERAAKEK VVSYMKEAGL AVYEDAVGNL
     IGRKEGKEKD APAVLVGSHI DSVYNGGMFD GPLGVLAAVE VLQTMNERGV KTKHPIEVVA
     FTDEEGARFS YGMIGSRGMA GTLSEEELVH QDKHGISLAA AMEEAGLDPG KIGKAARRKG
     SVKAYVELHI EQGRVLEQAN LPVGIVTGIA GLIWAKLTIT GKAEHAGATP MPIRRDPLVA
     AAQIIQVIEQ EAKKTGTTVG TVGQMQVFPG GINIIPERVE FSLDLRDLDA AVRDSVFLSI
     IERAKQIGNE RNVDVAVELL QKMPPVLCSE LVQNAAKEAC RQLGFDVFTL PSGASHDGVQ
     LAGLCPIGMI FVRSKDGVSH SPEEWSSKED CAAGANVLYH TVLSLAMTA
//

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