ID N6X068_9RHOO Unreviewed; 723 AA.
AC N6X068;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=B447_20538 {ECO:0000313|EMBL:ENO74986.1};
OS Thauera sp. 27.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=305700 {ECO:0000313|EMBL:ENO74986.1, ECO:0000313|Proteomes:UP000013140};
RN [1] {ECO:0000313|EMBL:ENO74986.1, ECO:0000313|Proteomes:UP000013140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=27 {ECO:0000313|EMBL:ENO74986.1,
RC ECO:0000313|Proteomes:UP000013140};
RA Liu B., Shapleigh J.P., Frostegard A.H.;
RT "Draft Genome Sequences of 6 Strains from Genus Thauera.";
RL Submitted (SEP-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENO74986.1}.
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DR EMBL; AMXB01000064; ENO74986.1; -; Genomic_DNA.
DR RefSeq; WP_002934063.1; NZ_AMXB01000064.1.
DR AlphaFoldDB; N6X068; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR Proteomes; UP000013140; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:ARBA00022628};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ENO74986.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013140}.
FT DOMAIN 592..723
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 723 AA; 78565 MW; ACE18113E3783291 CRC64;
MSQSNQSNEP TYNQADIEAW NKAAAKHAPG GDVTKLNWVT PEGLVVKPLY TKADTADLKH
ADTLPGFEPF LRGPQPTMYA VKPWTIRQYA GFSTAEASNA FYRKALAAGG QGVSVAFDLA
THRGYDSDHP RVTGDVGKAG VAIDSVEDMK ILFDGIPLDK ISVSMTMNGA VLPILAGYII
AAEEQGVSQD KLSGTIQNDI LKEFMVRNTY IYPPTPSMKI IADIFQYTSA NMPKFNSISI
SGYHIQEAGA NQAIELAFTL ADGLEYVRTG IASGMDVDTF AGRLSFFWAV GMNFYLEIAK
MRAARLLWWR IMKQFNPKSP KSMMLRTHSQ TSGWSLTEQD PYNNVVRTTI EAMAAVFGGT
QSLHTNALDE AIALPTEFSA RIARNTQIII QEETHICNVV DPWAGSYMME KLTQDMADKA
WALIEEIESM GGMTKAVESG WAKMKVEECA ADKQARIDSG KDVIVGVNKY KLAKEDPIEI
LDIDNHAVRE SQIARLAQVR ANRDTAAVQA ALDALTKCAE TGDGNLLDLT VKAIRLRATV
GEVSDALEKV FGRYRANPQA VSGVYGAVVE EQEDWKALKA DIEAFIAEEG RRPRVMIAKL
GQDGHDRGAK VVASAFADLG FDIDIGPLFQ TPEEAARHAV ENDVHAVGCS SLAAGHKTLV
PQIVNELKRL GADDIITFVG GVIPAQDYDA LYAAGAKGIF GPGTPIPTAA REVLKQIRAA
RKA
//