ID H2CBW6_9LEPT Unreviewed; 721 AA.
AC H2CBW6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=Lepil_3989 {ECO:0000313|EMBL:EHQ08638.1};
OS Leptonema illini DSM 21528.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptonema.
OX NCBI_TaxID=929563 {ECO:0000313|EMBL:EHQ08638.1, ECO:0000313|Proteomes:UP000005737};
RN [1] {ECO:0000313|EMBL:EHQ08638.1, ECO:0000313|Proteomes:UP000005737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21528 {ECO:0000313|EMBL:EHQ08638.1,
RC ECO:0000313|Proteomes:UP000005737};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.-M.,
RA Klenk H.-P., Eisen J.A.;
RT "The Improved High-Quality Draft genome of Leptonema illini DSM 21528.";
RL Submitted (OCT-2011) 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; JH597773; EHQ08638.1; -; Genomic_DNA.
DR RefSeq; WP_002775512.1; NZ_JH597773.1.
DR AlphaFoldDB; H2CBW6; -.
DR STRING; 183.GCA_002009735_02383; -.
DR HOGENOM; CLU_009523_3_1_12; -.
DR Proteomes; UP000005737; Unassembled WGS sequence.
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:InterPro.
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:UP000005737}.
FT DOMAIN 586..718
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 721 AA; 78997 MW; F589FD657C7FA38E CRC64;
MRPNFANIPY TKEPFAQISE EEFDRLLADD VWTTPEGIPV KPVYDRRALA GMEHLHYAAG
IAPFLRGPYP TMYTLQPWTI RQYAGFSTAE ESNAFYRRNL AAGQKGLSVA FDLATHRGYD
SDHPRVVGDV GMAGVAIDSV EDMKILFDQI PLDSVSVSMT MNGAVIPVLA FFIVAGEEQG
VPHEKLTGTI QNDILKEFMV RNTYIYPPAP SMQIIADIFA FTSKNMPKFN SISISGYHMQ
EAGATADIEL AYTLADGMEY IRTGLKAGLS IDEFAPRLSF FWAIGMNHFM EIAKMRAGRL
LWAKIVNSFG PKSAKSMALR THCQTSGWSL TEQDPFNNVT RTCVEALAAS LGHTQSLHTN
ALDEAIALPT DFSARIARNT QIYLQEETGI TKAIDPWAGS YYVETLTHML ARRAWKLIEE
VEGLGGIAKA IETGLPKMRI EEASARKQAR IDSGRDVIVG VNRFKADRDK PVDILAVDNT
AVRGAQIRRL EKIRAERNST DVEAALQAIT KCAETGQGNL LDLAVQAARK RATLGEISEA
MEKVFGRYRA VIRTISGVYS SEIMNDNSFK EAKDLADRFA KNEGRRPRIL VAKMGQDGHD
RGAKVVATSF ADIGFDVDVG PLFQTPEEVA KQAIENDVHI LGVSSLAGGH RTLVPQVIDE
LKRLGRDDIL VIAGGVIPHQ DYEALYKAGV AAVFGPGTVI ASAAAQLLKL LLGEDPASRS
A
//
