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Database: UniProt
Entry: Q8A5Z6_BACTN
LinkDB: Q8A5Z6_BACTN
Original site: Q8A5Z6_BACTN 
ID   Q8A5Z6_BACTN            Unreviewed;       715 AA.
AC   Q8A5Z6;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE            EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN   OrderedLocusNames=BT_2090 {ECO:0000313|EMBL:AAO77197.1};
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186 {ECO:0000313|EMBL:AAO77197.1, ECO:0000313|Proteomes:UP000001414};
RN   [1] {ECO:0000313|EMBL:AAO77197.1, ECO:0000313|Proteomes:UP000001414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
RN   [2] {ECO:0000313|EMBL:AAO77197.1, ECO:0000313|Proteomes:UP000001414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of its two
RT   dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000256|ARBA:ARBA00001922};
CC   -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC       {ECO:0000256|ARBA:ARBA00008465}.
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DR   EMBL; AE015928; AAO77197.1; -; Genomic_DNA.
DR   RefSeq; NP_811003.1; NC_004663.1.
DR   RefSeq; WP_008759796.1; NZ_UYXG01000035.1.
DR   AlphaFoldDB; Q8A5Z6; -.
DR   SMR; Q8A5Z6; -.
DR   STRING; 226186.BT_2090; -.
DR   PaxDb; 226186-BT_2090; -.
DR   EnsemblBacteria; AAO77197; AAO77197; BT_2090.
DR   GeneID; 60928078; -.
DR   KEGG; bth:BT_2090; -.
DR   PATRIC; fig|226186.12.peg.2151; -.
DR   eggNOG; COG1884; Bacteria.
DR   eggNOG; COG2185; Bacteria.
DR   HOGENOM; CLU_009523_3_1_10; -.
DR   InParanoid; Q8A5Z6; -.
DR   OrthoDB; 9762378at2; -.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031419; F:cobalamin binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IBA:GO_Central.
DR   GO; GO:0019678; P:propionate metabolic process, methylmalonyl pathway; IBA:GO_Central.
DR   CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR   CDD; cd03679; MM_CoA_mutase_alpha_like; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   Gene3D; 3.20.20.240; Methylmalonyl-CoA mutase; 1.
DR   InterPro; IPR006159; Acid_CoA_mut_C.
DR   InterPro; IPR016176; Cbl-dep_enz_cat.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
DR   InterPro; IPR006098; MMCoA_mutase_a_cat.
DR   NCBIfam; TIGR00640; acid_CoA_mut_C; 1.
DR   NCBIfam; TIGR00641; acid_CoA_mut_N; 1.
DR   PANTHER; PTHR48101:SF4; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48101; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF01642; MM_CoA_mutase; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   SUPFAM; SSF51703; Cobalamin (vitamin B12)-dependent enzymes; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS00544; METMALONYL_COA_MUTASE; 1.
PE   3: Inferred from homology;
KW   Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001414}.
FT   DOMAIN          586..715
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   715 AA;  78700 MW;  E577D1A1470025D7 CRC64;
     MRKDFKNLDI YAAFQPANGA EWQKANGISA DWNTPEHIDV KPVYTKEDLE GMEHLGYAAG
     LPPYLRGPYS VMYTLRPWTI RQYAGFSTAE ESNAFYRRNL ASGQKGLSVA FDLATHRGYD
     PDHERVVGDV GKAGVSICSL ENMKVLFDGI PLSKMSVSMT MNGAVLPIMA FYINAGLEQG
     AKLEEMAGTI QNDILKEFMV RNTYIYPPAF SMKIISDIFE YTSQKMPKFN SISISGYHMQ
     EAGATADIEL AYTLADGLEY LRAGTAAGID IDAFAPRLSF FWAIGTNHFM EIAKMRAARM
     LWAKIVKQFN PKNPKSLALR THSQTSGWSL TEQDPFNNVG RTCIEAMAAA LGHTQSLHTN
     ALDEAIALPT DFSARIARNT QIYIQEETYI CKNVDPWGGS YYVEALTNEL AHKAWERIEE
     VEKLGGMAKA IETGIPKMRI EEAAARTQAR IDSGSQTIVG VNKYRLEKEA PIDILEIDNT
     AVRLEQIENL KRLKEGRNQA EVDKALAAIT ECVETGKGNL LELAVEAARV RATLGEISYA
     CEKVVGRYKA IIRTISGVYS SESKNDGDFK RACELAEKFA KKEGRQPRIM VAKMGQDGHD
     RGAKVVATGY ADCGFDVDMG PLFQTPAEAA REAVENDVHV VGVSSLAAGH KTLIPQIMEE
     LKKLGREDIV VIAGGVIPAQ DYDFLYKAGV AAIFGPGTPV AKAACQILEI LMDEE
//
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