ID A0A2R8ALN5_9RHOB Unreviewed; 654 AA.
AC A0A2R8ALN5;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Methylmalonyl-CoA mutase {ECO:0000313|EMBL:SPF76955.1};
DE EC=5.4.99.2 {ECO:0000313|EMBL:SPF76955.1};
GN Name=scpA_3 {ECO:0000313|EMBL:SPF76955.1};
GN ORFNames=ALP8811_01972 {ECO:0000313|EMBL:SPF76955.1};
OS Aliiroseovarius pelagivivens.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Aliiroseovarius.
OX NCBI_TaxID=1639690 {ECO:0000313|EMBL:SPF76955.1, ECO:0000313|Proteomes:UP000244911};
RN [1] {ECO:0000313|EMBL:SPF76955.1, ECO:0000313|Proteomes:UP000244911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8811 {ECO:0000313|EMBL:SPF76955.1,
RC ECO:0000313|Proteomes:UP000244911};
RA Keele B.F.;
RL Submitted (MAR-2018) 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; OMOI01000001; SPF76955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8ALN5; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000244911; 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, ECO:0000313|EMBL:SPF76955.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000244911}.
FT DOMAIN 520..649
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 654 AA; 71564 MW; DA3AA8730D6DEDF0 CRC64;
MSSNTIRPWL FRTYAGHSTA KASNELYRTN LAKGQTGLSV AFDLPTQTGY DSDHKLSRGE
VGKVGVPLSH LGDMRALFDN IPLEQMNTSM TINATAPWLL SLYIAAAEEQ GADISKLQGT
VQNDIIKEYL SRGTYVCPPK PSLRMITDVA AYTREHLPKW NPMNVCSYHL QEAGATPEEE
LAFALATAIA VLDDLKEKVP AEAFPAMVGR ISFFVNAGIR FVTELCKMRA FVELWDEITR
ERYGVEDPKF RRFRYGVQVN SLGLTEQQPE NNVYRILIEM LAVTLSKNAR ARAVQLPAWN
EALGLPRPWD QQWSLRMQQI LAYETDLLEF DDLFDENPAV ERKVAELKDG ARAELAQIDG
MGGAVAAIEY MKSRLVDSNA ARIGKIEVGE TTVVGVNKWL ETTESPLTAG DGAIMVADKE
AEADQIARLE QWRADRDDAA VNDALSALRA AAKSGENIMH SSIAAAKAGV TTGEWGEVMR
QTFGQYRAPT GVSKNPSNRT EGLDEIRSRV DAVSDALGRR LNFLVGKPGL DGHSNGAEQI
AARARDCGMD ITYEGIRLTP EELVASALET KAHVVGLSIL SGSHIPLLEE LIERMKDAGL
GDVPVVAGGI IPDDDAERLR AMGVAKVYTP KDFELNTIME DIVTLVAPSS VAAE
//
