ID M3GSS8_LEPIR Unreviewed; 670 AA.
AC M3GSS8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Methylmalonyl-CoA mutase {ECO:0000313|EMBL:EMG09678.1};
DE EC=5.4.99.2 {ECO:0000313|EMBL:EMG09678.1};
GN ORFNames=LEP1GSC151_5641 {ECO:0000313|EMBL:EMG09678.1};
OS Leptospira interrogans serovar Grippotyphosa str. LT2186.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1001599 {ECO:0000313|EMBL:EMG09678.1, ECO:0000313|Proteomes:UP000011776};
RN [1] {ECO:0000313|EMBL:EMG09678.1, ECO:0000313|Proteomes:UP000011776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2186 {ECO:0000313|EMBL:EMG09678.1,
RC ECO:0000313|Proteomes:UP000011776};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Tulsiani S.M., Graham G.C., Burns M.-A.,
RA Dohnt M.F., Smythe L.D., McKay D.B., Craig S.B., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (FEB-2013) 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:EMG09678.1}.
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DR EMBL; AFME02000307; EMG09678.1; -; Genomic_DNA.
DR AlphaFoldDB; M3GSS8; -.
DR BioCyc; LINT1001599:G11K9-2350-MONOMER; -.
DR Proteomes; UP000011776; 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:UniProtKB-EC.
DR CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR CDD; cd03681; MM_CoA_mutase_MeaA; 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:SF3; COENZYME B12-DEPENDENT MUTASE; 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.
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:EMG09678.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 538..666
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 670 AA; 74848 MW; 93477F049FE1E63C CRC64;
MENKNHILYD KSGKPSKEPA WIFRTYAGHT NARESNELFR KNLSKGQTGL SIAFDLATQC
GYSSDHPIAK PEIGKVGVPI NTLEDFRILF NQIPIEEMNT SMTINGTSMY LLSLYVALAQ
ERGVDVSLLQ GTTQNDIIKE YLARGTYIFP PAQSIRIIVD MYEYCLKNIP KWNPSNICSY
HLQEAGATPV QELAFALATA MAILDAIKER NCFTPDEFEQ CVGRISFFVN AGIRFVEEMC
KMRAFTEMWD EITKDRYGVK QDKYRRFRYG VQVNSLGLTE EQPENNAWRI LIEALGVTMS
RDARCRALQL PAWNEALSLP RPWDQQWSLR LQQVLAYETD LLEYPDLFEG SKVVESKVKE
LKEEAYKEIQ KILDMGGAIQ AIENGYMKSQ LVKSQAERLA KINNNEMVIV GKNKWTEGIA
SPLMTDQDGG VFKVDSKSAE ETLEVLAKVK SNRDTNQVKA ALAQLEADAK AGKNLMYASI
ECAKVGISTG EWADVLRSVF GEYRPATGVE GQKLNLESEK VTRVRGKVEA FLKTNGSRPK
IVVGKPGLDG HSNGAEMIAV SAKHAGFDVI YSGIRLTPEE IVQTAVEENA DVIGVSILSG
SHLELAEQIF NELKHYKADI PVVFGGIIPP SDFETLTKLG VKAIFTPKDY DLMDVMERII
DIISKTVKAA
//
