ID A0A0C1RJB7_9ACTN Unreviewed; 709 AA.
AC A0A0C1RJB7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=MB52_04970 {ECO:0000313|EMBL:KIE50741.1};
OS marine actinobacterium MedAcidi-G1.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1550399 {ECO:0000313|EMBL:KIE50741.1, ECO:0000313|Proteomes:UP000031399};
RN [1] {ECO:0000313|EMBL:KIE50741.1, ECO:0000313|Proteomes:UP000031399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mizuno C.M., Rodriguez-Valera F., Ghai R.;
RT "Novel reconstructed genomes of marine planktonic Acidimicrobiales.";
RL Submitted (SEP-2014) 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:KIE50741.1}.
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DR EMBL; JUEM01000012; KIE50741.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1RJB7; -.
DR Proteomes; UP000031399; 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.
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:KIE50741.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 583..709
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 709 AA; 77899 MW; F48CF953226800E1 CRC64;
MTKIPNFSKI EFDQNPETNN NESQHNGELW ETAEKISIKN CYTHKDIENL DFLNGWPGLA
PFLRGPHATM YKTRPWTIRQ YGGFSTAEES NAFYRRNLED GQRGISVAFD LATHRGYDSD
HPRVAGDVGM AGVAIDSILD MQKLFDGIPL DKMSVSMTMN GAVLPIMALY IVAAEEQGVP
AKALTGTIQN DILKEFMVRN TYIYPPEPSM RIISDIFAYT SAEMPRFNSI SVSGYHMQEA
GATADLELAY TLADGIEYVR AGLKAGLDVD SFSPRISFFW GIGMNFFMEV AKMRAARLIW
ARLMSQFEPK DDRSLSLRTH CQTSGWSLTA QDPYNNVIRT CIEAMAATQG HTQSLHTNSF
DEALALPTDF SAKIARDTQA FLQEETDSCR VIDPWGGSYY LERLTKDLAE KAMDHIYEIE
NSGGMAKAIE AGIPKLRIEE AAARTQARID SGQQSVIGVN RYRPETESIV NVLRVDNAEV
RASQIAQLEE LKATRDQNQC QIALEELTNA AEKNENLLAA SVKAARARAT VGEISDALEK
IFGRHRAEVR TISGVFSSEV GDNEDVQAVR DRANKFEADS GRRPRILVAK IGQDGHDRGQ
KVIATAFADL GFDVDIGPLF ATPSETAMQA VENDVHVVGV SSLAAGHLTL VPQLKKELES
LGRSDIAIVV GGVIPPDDFD ALQDAGVAAV FPSGTVIAEA AIELLEKLS
//
