ID A0A0M8XCW6_9ACTN Unreviewed; 741 AA.
AC A0A0M8XCW6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=ADK66_28790 {ECO:0000313|EMBL:KOX03198.1};
OS Micromonospora sp. NRRL B-16802.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1415541 {ECO:0000313|EMBL:KOX03198.1, ECO:0000313|Proteomes:UP000037709};
RN [1] {ECO:0000313|EMBL:KOX03198.1, ECO:0000313|Proteomes:UP000037709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16802 {ECO:0000313|EMBL:KOX03198.1,
RC ECO:0000313|Proteomes:UP000037709};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOX03198.1}.
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DR EMBL; LGEB01000121; KOX03198.1; -; Genomic_DNA.
DR RefSeq; WP_053660850.1; NZ_LGEB01000121.1.
DR AlphaFoldDB; A0A0M8XCW6; -.
DR STRING; 1415541.ADK66_28790; -.
DR PATRIC; fig|1415541.3.peg.6035; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000037709; 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; 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, ECO:0000313|EMBL:KOX03198.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 607..739
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 741 AA; 79919 MW; 0CCAD478F5AE6782 CRC64;
MGVGIPDFSE VELGGPATAA DADLGRWHDA VRAETGSDPQ ELTWQTPEGI DVAPLHTAAD
RDGLDFLGTF PGIAPYLRGP YPTMYTTQPW TVRQYAGFST AQESNAFYRR NLAAGQKGLS
VAFDLPTHRG YDSDHPRVAG DVGMAGVAID SIYDMRQLFD GIPLDRMSVS MTMNGAVLPV
LALYIVAAEE QGVAPEQLSG TIQNDILKEF MVRNTYIYPP QPSMRIISDI FAFTSERMPR
FNSISISGYH IQEAGATADL ELAYTLADGV EYLRAGRDAG LDIDAFAPRL SFFWAIGMNF
FMEVAKLRAA RLLWARLVRD FQPKNPKSLS LRAHSQTSGW SLTAQDVFNN VVRTCVEAMA
ATQGHTQSLH TNALDEALAL PTDFSARIAR NTQLLLQQES GTTRVIDPWG GSAYVERLTH
DLAARAWKHI QEVEAAGGMA RAIDEGIPKL RIEGAAARTQ ARIDSGRQPV IGVNKYRPDA
DEPIDVLKVD NRSVRAQQIE KLRRLREERD EQTCVAALDA LTRAAGAALD GTRGPGLDGN
LLALAVDAAR AKATVGEISD AMEKVYGRHA AQIRTISGVY RDEAGAVSAI ESVRAATAEF
AVAEGRQPRI LVAKMGQDGH DRGQKVIATA FADLGFDVDV GPLFQTPAEV ARQAVEADVH
IVGVSSLAAG HLTLVPALRD ELAALDRDDI MIIVGGVIPP QDFDALRAAG AAAIFPPGTV
IAEAARELLT ELSRRLGHPG A
//
