ID A0A1B2AE76_9SPHN Unreviewed; 715 AA.
AC A0A1B2AE76;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN Name=scpA_1 {ECO:0000313|EMBL:ANY20401.1};
GN ORFNames=A6F68_01891 {ECO:0000313|EMBL:ANY20401.1};
OS Tsuneonella dongtanensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Tsuneonella.
OX NCBI_TaxID=692370 {ECO:0000313|EMBL:ANY20401.1, ECO:0000313|Proteomes:UP000092932};
RN [1] {ECO:0000313|EMBL:ANY20401.1, ECO:0000313|Proteomes:UP000092932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22672 {ECO:0000313|EMBL:ANY20401.1,
RC ECO:0000313|Proteomes:UP000092932};
RA Cheng H., Wu Y.-H., Zhou P., Huo Y.-Y., Wang C.-S., Xu X.-W.;
RT "Complete genome sequence of Altererythrobacter dongtanensis KCTC 22672, a
RT type strain with esterase isolated from tidal flat.";
RL Submitted (JUL-2016) 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}.
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DR EMBL; CP016591; ANY20401.1; -; Genomic_DNA.
DR RefSeq; WP_067679030.1; NZ_CP016591.1.
DR AlphaFoldDB; A0A1B2AE76; -.
DR STRING; 692370.A6F68_01891; -.
DR KEGG; ado:A6F68_01891; -.
DR PATRIC; fig|692370.5.peg.1905; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000092932; Chromosome.
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:ANY20401.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000092932}.
FT DOMAIN 574..706
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 715 AA; 76689 MW; 186F377DEC296191 CRC64;
MTDKTRDDWQ ALADKEVKGR DLTWHTPEGF AIQPLYTADD VPADPGLPGF APFTRGVKAS
MYAGRPWTIR QYAGFSTAEE SNAFYRRNLA MGQKGLSVAF DLATHRGYDS DHPRVVGDVG
KAGVAIDTVR DMEILFDGIP LDQMSVSMTM NGAVIPVLAF FIVAAERQGV SRDKLDGTIQ
NDILKEFMVR NTYIYPPEPS MRIVSDIIAY TSAEMPKFNS ISISGYHMHE AGATAVQELA
FTIADGKEYA TRAMAAGLDI DAFAGRLSFF FGIGMNFFME VAKLRAARTL WWKTMNGLGA
KSERSKMLRT HCQTSGVSLQ EQDPYNNVIR TTIEALASVL GGTQSLHTNA LDEAIALPTD
FSARIARNTQ LVLQEETGIT NVVDPLGGSY YVEALTAKLV EEAEKLIAEV DAAGGMTAYV
ASGKPKAAIE SAAAAKQASV DRGETVIVGV NKYRKAEEEH LDTLDIDNHA VREAQIARLK
AVRAGRDEAA CQAALKALTE GCTNGGNLLA LAVEAARHDA TLGEISAAME EAFGRYGTNP
TPVKGIYSAA YEGDSRYAQV VEGVAAVGRR LGRAPKVLVA KMGQDGHDRG ANVIASAFAD
MGFDVVSGPL FQTPAETRDM ALAEKVDAIG ASSLAAGHKT LIPELIGLLR EAGRPDIKVV
AGGVIPPQDY DFLREAGVQG IYGPGSKVVE CAADMLRLLG HNMPPIGSEL REKAK
//
