ID   A0A2A5CE43_9GAMM        Unreviewed;       672 AA.
AC   A0A2A5CE43;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Protein meaA {ECO:0000313|EMBL:PCJ42032.1};
GN   ORFNames=COA99_08505 {ECO:0000313|EMBL:PCJ42032.1};
OS   Moraxellaceae bacterium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae.
OX   NCBI_TaxID=1889775 {ECO:0000313|EMBL:PCJ42032.1, ECO:0000313|Proteomes:UP000218379};
RN   [1] {ECO:0000313|Proteomes:UP000218379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) 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:PCJ42032.1}.
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DR   EMBL; NVVG01000066; PCJ42032.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A5CE43; -.
DR   Proteomes; UP000218379; 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:InterPro.
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}.
FT   DOMAIN          539..669
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   672 AA;  74832 MW;  E0F7877E066C530A CRC64;
     MTDNQKHLLT DKDGKATKDR PWIFRTYAGH TNVRKSNELY RSNLAKGQTG LSIAFDLATQ
     CGYSSDEEIA KPEIGKVGVP INTLDDFAIL FDQIDIAEVN TSMTINGTSM WLLSLYIALA
     EERGVPIDQL QGTTQNDLIK EFLARGTYVF PPEESIKLIV DMYEYCLTNV PKWNPSNVCS
     YHLQEAGATP VKELAYSLVT AITVLDAIKE RNCFNEDEFE RCVGRVSFFV NAGMRFIEEM
     CKMRAFTQLW DEICIERYKV KNPKFRRFRY GIQVNSLGLT EEQPENNAWR ILIETLGVTL
     SRDARCRALQ LPAWNEALSL PRPWDQQWSL RLQQILAYET DLLEYPDLFD GSPVIESKVN
     ELKEQAWAEI QKILDAGGGV EAIKNGYMKS QLVISQADRM SKINSGEHIV VGKNRWTEGI
     ESPLVRDSDG GVFKVDPESA AETLSALAET KAKRDSAKAE ECLRVLKETA QQGGNLMLAS
     IACAKARVTT GEWTATLRDV YGEYRPPTGV EGQSLSIENE TLDTVRAKVA TFMEKSGHRP
     RIVVGKPGLD GHSNGAEMIS VAARHAGFDV IYFGIRLSAT DIVQSAIEED VDVIGISLLS
     GSHNEIMDQL FEELEAEGAK GSIPVVLGGI IPQADAEALT KKGVRAIFTP KDYDLMEVMN
     RIMDVILEDT AK
//