ID A9C2N6_DELAS Unreviewed; 738 AA.
AC A9C2N6;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN OrderedLocusNames=Daci_3753 {ECO:0000313|EMBL:ABX36385.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX36385.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX36385.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) 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; CP000884; ABX36385.1; -; Genomic_DNA.
DR AlphaFoldDB; A9C2N6; -.
DR STRING; 398578.Daci_3753; -.
DR KEGG; dac:Daci_3753; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_3_1_4; -.
DR Proteomes; UP000000784; 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:ABX36385.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000784}.
FT DOMAIN 607..738
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 80033 MW; ED1897F3B6701049 CRC64;
MPSRAPVIHE PENMRQDHPT AQNGQEFATA DLQKWAQAAA KAAPGGDIQA LHWTTPDGID
VKPLYTAADT ANLPHTDSLP GFEPYIRGPQ ATMYAGRPWT IRQYAGFSTA EESNAFYRKA
LAAGGQGVSV AFDLATHRGY DSDHPRVTGD VGKAGVAIDS VEDMKVLFDQ IPLDKISVSM
TMNGAVLPVL AGYVVAAEEQ GVAQDQLSGT IQNDILKEFM VRNTYIYPPQ PSMRIIGDII
EYTSRNMPKF NSISISGYHM QEAGANQALE LAFTLADGKE YVKTATAKGM DVDDFAGRLS
FFWAIGMNFY LEIAKMRAAR LLWCRIMKGF GAKKAKSLML RTHCQTSGWS LTEQDPYNNV
VRTTIEAMAA VFGGTQSLHT NSFDEAIALP TEFSARIARN TQLIIQEETH ITNVIDPWAG
SYMMEKLTQD MADAAWKIIE EVEAMGGMTA AVDSGWAKLK IEAAAAEKQA RIDSGKDVIV
GVNKYKLAKE DAIDILEVDN VKVRDSQIAR LNQIKASRDA AKVEAALQAL TQAAESGEGN
LLDLAIQAVR LRATVGEVSD ALEKVFGRHR ADTQKVTGVY AAAYDSAEGW EKLKGEIDAS
SEQLGRRPRV MIAKLGQDGH DRGAKVVATA FADLGFDVDM GPLFQTPEEC ARQAIENDVH
AVGVSTLAAG HKTLVPAIIE ELRRQGADDI IVFVGGVIPA QDYDFLYNAG VKGVYGPGTP
IPASAKDVLE QIRQANSL
//
