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Database: UniProt
Entry: A5N4X5_CLOK5
LinkDB: A5N4X5_CLOK5
Original site: A5N4X5_CLOK5 
ID   A5N4X5_CLOK5            Unreviewed;       430 AA.
AC   A5N4X5;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=MutE {ECO:0000313|EMBL:EDK32356.1};
DE            EC=5.4.99.1 {ECO:0000313|EMBL:EDK32356.1};
GN   Name=mutE {ECO:0000313|EMBL:EDK32356.1};
GN   OrderedLocusNames=CKL_0302 {ECO:0000313|EMBL:EDK32356.1};
OS   Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK32356.1, ECO:0000313|Proteomes:UP000002411};
RN   [1] {ECO:0000313|EMBL:EDK32356.1, ECO:0000313|Proteomes:UP000002411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680
RC   {ECO:0000313|Proteomes:UP000002411};
RX   PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA   Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA   Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA   Hagemeier C., Thauer R.K., Gottschalk G.;
RT   "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT   metabolic features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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DR   EMBL; CP000673; EDK32356.1; -; Genomic_DNA.
DR   RefSeq; WP_011988871.1; NC_009706.1.
DR   AlphaFoldDB; A5N4X5; -.
DR   STRING; 431943.CKL_0302; -.
DR   KEGG; ckl:CKL_0302; -.
DR   eggNOG; COG4865; Bacteria.
DR   HOGENOM; CLU_029922_0_0_9; -.
DR   Proteomes; UP000002411; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0050097; F:methylaspartate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019670; P:anaerobic glutamate catabolic process; IEA:InterPro.
DR   Gene3D; 3.90.970.10; -; 1.
DR   Gene3D; 3.20.20.240; Methylmalonyl-CoA mutase; 1.
DR   InterPro; IPR016176; Cbl-dep_enz_cat.
DR   InterPro; IPR006396; Glu_mut_E.
DR   InterPro; IPR014714; Glu_mut_E_C_dom_sf.
DR   NCBIfam; TIGR01503; MthylAspMut_E; 1.
DR   Pfam; PF06368; Met_asp_mut_E; 1.
DR   PIRSF; PIRSF001495; Met_asp_mut_epsi; 1.
DR   SUPFAM; SSF51703; Cobalamin (vitamin B12)-dependent enzymes; 1.
PE   4: Predicted;
KW   Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:EDK32356.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002411}.
SQ   SEQUENCE   430 AA;  47811 MW;  9112772ABA9348E8 CRC64;
     MKLKNEKWPE EYFFKTRNKI LNYDIKGAVD YLRKVPDYKN FSKRLIAAKE DFITLIQPGM
     ANIPEERLGL LKYLQDEGKP DLLLVSMYNS VAQNENNSSS NLKYFIEECR EICESVDLPI
     QGTYNTFDCK LLAEIICLCG FTSSQGGAIS HNILNATNIP IEKSILDWQY CDRLVGFYEE
     QGISINKETF GVANYNALIP PSISNAVSII EGLLAAEQGV KNITVGITQG GNLIQDIASI
     KALEEQIGEY MKDYGYKDVY ITTSFHQSML KSSEDKGKNF GTTSVGTVTA VLAGATKVVI
     KTSKLTKEVN SAIIRAAKMP VDILGGQRLA MSKELETEVV IIKAEVKCIL DKVLELGRGD
     LAVGVVEAFE NGVIDIPVAS ERYSKDGGMT SARDNTGAIR YMRFGNIPFT QELKNFNKRK
     MEGKNIKNKF
//
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