(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BI08_GEOS0

ID   A0A0F6BI08_GEOS0        Unreviewed;       358 AA.
AC   A0A0F6BI08;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 29.
DE   RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE            EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN   OrderedLocusNames=GY4MC1_0210 {ECO:0000313|EMBL:ADP73059.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73059.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73059.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73059.1,
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU366006};
CC       Note=Binds 1 Mg(2+) ion per subunit.
CC       {ECO:0000256|RuleBase:RU366006};
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. {ECO:0000256|RuleBase:RU366006,
CC       ECO:0000256|SAAS:SAAS01080498}.
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DR   EMBL; CP002293; ADP73059.1; -; Genomic_DNA.
DR   RefSeq; WP_013399867.1; NC_014650.1.
DR   EnsemblBacteria; ADP73059; ADP73059; GY4MC1_0210.
DR   KEGG; gmc:GY4MC1_0210; -.
DR   KO; K19802; -.
DR   OMA; CYSDSSL; -.
DR   OrthoDB; 951991at2; -.
DR   BioCyc; GSP581103:G1GOQ-252-MONOMER; -.
DR   Proteomes; UP000002034; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016855; F:racemase and epimerase activity, acting on amino acids and derivatives; IEA:UniProtKB-UniRule.
DR   CDD; cd03319; L-Ala-DL-Glu_epimerase; 1.
DR   Gene3D; 3.20.20.120; -; 1.
DR   Gene3D; 3.30.390.10; -; 1.
DR   InterPro; IPR034603; Dipeptide_epimerase.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BI08.
DR   SWISS-2DPAGE; A0A0F6BI08.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Isomerase {ECO:0000256|RuleBase:RU366006};
KW   Magnesium {ECO:0000256|RuleBase:RU366006};
KW   Metal-binding {ECO:0000256|RuleBase:RU366006,
KW   ECO:0000256|SAAS:SAAS01101683}.
FT   DOMAIN      141    239       MR_MLE. {ECO:0000259|SMART:SM00922}.
SQ   SEQUENCE   358 AA;  39443 MW;  F87D8C07C3C3E9AC CRC64;
     MKIKDATIAV QSTPLIKPFK TALRTATQIE SIVVKITLDN GMEGYGAAVP TEAITGETKQ
     GIIGVLENVL IPKIIGREIE EINKNDKDIQ TSCIGNTSAK AALEMAMYDA LCKLLNIPLY
     QLFGGKMNHH VNDMTISVNN VEEMVNDAKK VTEKGFSILK IKVGKEAEKD IERIERIYDE
     VGPNISLRID ANQGWTAKDA VKIIQSLEQL HLPIEFIEQP VSKHDIKGLQ FIRERVNVPI
     MADESVFSAR DALELIRHHA VDLINIKLMK TGGLREAYKI ASLAEAAGIE CMIGSMMEPT
     LSVLAAAHLA MAHPNITKVD LDAPLWINDD SSRSFFQESK INVPDLPGIG YVPSMPNH
//

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