ID M6GCM7_LEPIR Unreviewed; 670 AA.
AC M6GCM7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Methylmalonyl-CoA mutase {ECO:0000313|EMBL:EMM82718.1};
DE EC=5.4.99.2 {ECO:0000313|EMBL:EMM82718.1};
GN ORFNames=LEP1GSC037_3392 {ECO:0000313|EMBL:EMM82718.1};
OS Leptospira interrogans str. 2006001854.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1001590 {ECO:0000313|EMBL:EMM82718.1, ECO:0000313|Proteomes:UP000012128};
RN [1] {ECO:0000313|EMBL:EMM82718.1, ECO:0000313|Proteomes:UP000012128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2006001854 {ECO:0000313|EMBL:EMM82718.1,
RC ECO:0000313|Proteomes:UP000012128};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Hospenthal D.R., Murray C.K., Pimentel G.,
RA Wasfy M., Parker T., Miller R.S., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA Fouts D.E.;
RL Submitted (JAN-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:EMM82718.1}.
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DR EMBL; AFLW02000079; EMM82718.1; -; Genomic_DNA.
DR AlphaFoldDB; M6GCM7; -.
DR Proteomes; UP000012128; 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:EMM82718.1};
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; 74864 MW; 3C12F495A02BE8C8 CRC64;
MENKNHILYD KSGKPSKEPA WIFRTYAGHT NARESNDLFR 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 TLAQLEADAK AGKNLMYASI
ECAKVGISTG EWADVLRSVF GEYRPATGVE GQKLNLESEK VTRVRGKVEA FLKTNGSRPK
IVVGKPGLDG HSNGAEMIAV SAKHAGFDVI YSGIRLTPEE IVQTAVEENA DVIGVSILSG
SHLELAEQIF NELKHYKADI PVVFGGIIPP SDFETLTKLG VKAIFTPKDY DLMDVMERII
DIISKTVKAA
//
