ID A9MRG0_SALAR Unreviewed; 714 AA.
AC A9MRG0;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN OrderedLocusNames=SARI_04585 {ECO:0000313|EMBL:ABX24358.1};
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514 {ECO:0000313|EMBL:ABX24358.1, ECO:0000313|Proteomes:UP000002084};
RN [1] {ECO:0000313|EMBL:ABX24358.1, ECO:0000313|Proteomes:UP000002084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980
RC {ECO:0000313|Proteomes:UP000002084};
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) 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; CP000880; ABX24358.1; -; Genomic_DNA.
DR AlphaFoldDB; A9MRG0; -.
DR STRING; 41514.SARI_04585; -.
DR KEGG; ses:SARI_04585; -.
DR HOGENOM; CLU_009523_3_1_6; -.
DR Proteomes; UP000002084; 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:InterPro.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002084}.
FT DOMAIN 584..714
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 714 AA; 77563 MW; E8508A135048E317 CRC64;
MANLQAWQTL ANNELSRREK TVESLIRQTA EGIAVKPLYT EADLNNLEVT GTLPGLPPYV
RGPRATMYTA QPWTIRQYAG FSTAKESNAF YRRNLAAGQK GLSVAFDLAT HRGYDSDNPR
VAGDVGKAGV AIDTVEDMKV LFDQIPLDKM SVSMTMNGAV LPVMAFYIVA AEEQGVSPEQ
LTGTIQNDIL KEYLCRNTYI YPPKPSMRII ADIIAWCSGN MPRFNTISIS GYHMGEAGAN
CVQQVAFTLA DGIEYIKAAL SAGLKIDDFA PRLSFFFGIG MDLFMNVAML RAARYLWSEA
VSGFGATNPK SLALRTHCQT SGWSLTEQDP YNNIIRTTIE ALGATLGGTQ SLHTNAFDEA
LGLPTDFSAR IARNTQIIIQ EESSICRTVD PLAGSYYVES LTDQIVKQAR AIIKQIDAAG
GMAKAIEAGL PKRMIEEASA REQSLIDQGE RVIVGVNKYK LEKEDETAVL EIDNVKVRNE
QIAALERIRA TRDNRAVNAA LQALTHAAQH HENLLAAAVE AARVRATLGE ISDALEAAFD
RYLVPSQCVT GVIAQSYHQS DKSAGEFDAI VAQTQQFLAD TGRRPRILIA KMGQDGHDRG
AKVIASAYSD LGFDVDLSPM FSTPDEIARL AVENDVHVIG ASSLAAGHKT LIPELVAALK
KWGREDICVV AGGVIPPQDY AFLKAHGVAA IYGPGTPMLE SVRDVLARIS QHHD
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