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Database: UniProt
Entry: B3EIB7_CHLL2
LinkDB: B3EIB7_CHLL2
Original site: B3EIB7_CHLL2 
ID   B3EIB7_CHLL2            Unreviewed;       715 AA.
AC   B3EIB7;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE            EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN   OrderedLocusNames=Clim_0868 {ECO:0000313|EMBL:ACD89947.1};
OS   Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290315 {ECO:0000313|EMBL:ACD89947.1, ECO:0000313|Proteomes:UP000008841};
RN   [1] {ECO:0000313|EMBL:ACD89947.1, ECO:0000313|Proteomes:UP000008841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 245 / NBRC 103803 / 6330
RC   {ECO:0000313|Proteomes:UP000008841};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium limicola DSM 245.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001097; ACD89947.1; -; Genomic_DNA.
DR   RefSeq; WP_012465826.1; NC_010803.1.
DR   AlphaFoldDB; B3EIB7; -.
DR   STRING; 290315.Clim_0868; -.
DR   KEGG; cli:Clim_0868; -.
DR   eggNOG; COG1884; Bacteria.
DR   eggNOG; COG2185; Bacteria.
DR   HOGENOM; CLU_009523_3_1_10; -.
DR   OrthoDB; 9762378at2; -.
DR   Proteomes; UP000008841; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:ACD89947.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          583..715
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   715 AA;  79072 MW;  E540A5CA5E9AC0B4 CRC64;
     MRPDFSEIDI FSLPEETPSA AEIPVAENWT TAEGIGIRSR YTARDIEKAD HLHFAPGFPP
     YAGGPYSTMY TTRPWTIRQY AGFSTAEESN AFYRKNLSAG QKGLSVAFDL PTHRGYDSDH
     ERVIGDVGKA GVAVDSVEDM KILFDRIPLD DISVSMTMNG AVLPVMAFYI VAAEEQGVPV
     EKLSGTIQND ILKEFMVRNT YIYPPEPSMR IIGDIFRYTS GRMPKFNSIS ISGYHMQEAG
     ATADLELAYT LADGLEYIRT GLKSGLDIDS FAPRLSFFWA VGMNYFMEIA KLRAARMLWA
     KIVSGFNPKN PKSLMLRSHC QTSGWSLTEQ DPYNNIARTC IEALAATLGH TQSLHTNALD
     EAIALPSPFS ARIARNTQLY LQEETDITRC IDPWAGSHYV EYLTGELAEK TWKIISEIEE
     AGGMVKAIEQ GLPKLRIEEA ATRKQARIDC GEDIIVGVNG YTTSSSTDID LLEVDNTMVL
     QQQVDRLKRI RAERNSEETA SALQAIESCA ENGTGNLLEL AVDAARKRAT LGEISSACEK
     VFGRYRSSIR LNTNVYRSQM QHNRLFQEAQ ELADRFASLE GRRPRIMVAK VGQDGHDRGA
     KVISAGFADI GFDVDISPLF QTPEEVVRQA LDNDVHLIGI SSLAAGHKTL IPKIIESLRD
     AHREDILVVA GGIIPERDHA FLYQQGVAGI FGPGTVIADA AVKILKLLLA KFEHE
//
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