(data stored in ACNUC7421 zone)

SWISSPROT: B4SHK1_STRM5

ID   B4SHK1_STRM5            Unreviewed;       364 AA.
AC   B4SHK1;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE            EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN   OrderedLocusNames=Smal_0339 {ECO:0000313|EMBL:ACF50044.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50044.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50044.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50044.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) 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; CP001111; ACF50044.1; -; Genomic_DNA.
DR   RefSeq; WP_004139139.1; NC_011071.1.
DR   STRING; 391008.Smal_0339; -.
DR   EnsemblBacteria; ACF50044; ACF50044; Smal_0339.
DR   KEGG; smt:Smal_0339; -.
DR   eggNOG; ENOG4105DTQ; Bacteria.
DR   eggNOG; COG4948; LUCA.
DR   HOGENOM; HOG000185903; -.
DR   KO; K19802; -.
DR   OMA; LDYVDMD; -.
DR   OrthoDB; 951991at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01770-MONOMER; -.
DR   Proteomes; UP000001867; 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   SFLD; SFLDF00010; dipeptide_epimerase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4SHK1.
DR   SWISS-2DPAGE; B4SHK1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
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   364 AA;  38823 MW;  B4D55F972C562D9C CRC64;
     MKITAIELGM LRVPLKTPFK TALRTVETVE DVVVLIRTDT GHTGYGEAPA TAVITGDTHG
     SIIEAIRHFI APRLIGQDVV NLNHLCTLVQ TAMERNSSAK AAVEIALYDL WAQLHGAPLY
     QMLGGGDPVI TTDITISVDY IDKMVADSLS AIERGFESLK IKVGKDIGLD IERVKAIHAA
     VEGRALLRLD ANQGWTAKQA VHAMRTLEEA GVVLELLEQP VKAADISGLK YVTDRVNTPV
     MADESVFSPS QVMDLIQQRA ADIINIKLMK TGGLSNAIRI ADIAGIYGVP CMIGCMIESS
     ISVAAAVHLA VAKSDVITKV DLDGPSLGQF DPVSGGVHFN ESEISISDVP GLGITEVRGL
     EMLG
//

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