ID K6WPC1_9MICO Unreviewed; 687 AA.
AC K6WPC1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN Name=meaA {ECO:0000313|EMBL:GAB95671.1};
GN ORFNames=KILIM_025_00070 {ECO:0000313|EMBL:GAB95671.1};
OS Kineosphaera limosa NBRC 100340.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Kineosphaera.
OX NCBI_TaxID=1184609 {ECO:0000313|EMBL:GAB95671.1, ECO:0000313|Proteomes:UP000008366};
RN [1] {ECO:0000313|EMBL:GAB95671.1, ECO:0000313|Proteomes:UP000008366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100340 {ECO:0000313|EMBL:GAB95671.1,
RC ECO:0000313|Proteomes:UP000008366};
RA Yoshida I., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y.,
RA Ohji S., Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Kineosphaera limosa NBRC 100340.";
RL Submitted (AUG-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 -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
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:GAB95671.1}.
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DR EMBL; BAHD01000025; GAB95671.1; -; Genomic_DNA.
DR RefSeq; WP_006592203.1; NZ_BAHD01000025.1.
DR AlphaFoldDB; K6WPC1; -.
DR STRING; 1184609.KILIM_025_00070; -.
DR eggNOG; COG2185; Bacteria.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000008366; 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 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008366}.
FT DOMAIN 546..675
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 687 AA; 73820 MW; A90AFD9E376DDDB9 CRC64;
MGERTKPWVM RTYAGHSSAA ASNELYRRNL AKGQTGLSVA FDLPTQTGYD PDDELARGEV
GKVGVPVSHI GDMRALFAGI PLAQMNTSMT INAPAMWLLA LYEAVAREQA DEAGADADDV
VRGLGGTTQN DIIKEYLSRG THVFPPGPSL RLTGDTIAYT LVNMPKWNPV NICSYHLQEA
GATPVQEVAF AMATATEILD QVQARGLVPP ERFGEVVARI SFFVNAGVRF VEEMCKMRAF
VQLWDELTRE RYGVTDPKHR RFRYGVQVNS LGLTEAQPEN NIQRIVLEML GVTLSKDARA
RAVQLPAWNE ALGLPRPWDQ QWSLRMQQVL AYESDLLEYD DLFTGSVVVE AKVEQIVTEA
KKLMARIEEM GGAVAAVESG FLKGELVASH ARRRRRIEGG DEIVVGVNAF TTTEPSPLTE
NLDTAIHRVD PGVEAAAREA VAAWRTERDA DPARAQEAAE ALTQLSRDAA DASVNLMPAT
VRCARAGVTT GEWAQALREV FGEFRAPTGV SGAVSSADGA EDSASAQRTR AVQQAVRETG
EALGGPLRLL VGKPGLDGHS NGAEQVAVRA RDVGFEVVYQ GIRLRPSEIV AAAVAEDVHC
VGISVLSGSH NELVPEILDG LRDAGAGDVP VVVGGIIPAA DEARLLQLGV AAVFTPKDHD
LTACMGRIVD AIRAANGLSV DRVLESA
//
