ID A0A316TMZ6_9ACTN Unreviewed; 716 AA.
AC A0A316TMZ6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=DJ010_02945 {ECO:0000313|EMBL:PWN04599.1};
OS Nocardioides silvaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=2201891 {ECO:0000313|EMBL:PWN04599.1, ECO:0000313|Proteomes:UP000245507};
RN [1] {ECO:0000313|EMBL:PWN04599.1, ECO:0000313|Proteomes:UP000245507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB 2018079 {ECO:0000313|EMBL:PWN04599.1,
RC ECO:0000313|Proteomes:UP000245507};
RA Li C., Wang G.;
RT "Nocardioides silvaticus genome.";
RL Submitted (MAY-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 -!- 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:PWN04599.1}.
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DR EMBL; QGDD01000001; PWN04599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316TMZ6; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000245507; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000245507}.
FT DOMAIN 585..716
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 716 AA; 77765 MW; D2847CE51592E96C CRC64;
MSIPKSFAGL PLTGDAASAV PVHGDLESWH SPEGIEIKPS YDASDLTGLD ALDTWPGLSP
FLRGPYPTMY TTQPWTIRQY AGFSTAEESN AFYRRNLAAG QKGLSVAFDL ATHRGYDSDH
PRVRGDVGMA GVAIDSIYDT RTLFDGIPLD QMSVSMTMNG AVLPVLALYI AAGEEQGVKP
EQLSGTIQND ILKEFMVRNT YIYPPAPSMR IISDIFAFTS QRMPRFNSIS ISGYHMQEAG
ATADLELAYT LADGVEYIRA GLESSLTIDQ FAPRLSFFWA IGMNFYMEVA KMRAARAIWS
RLVRQFDPQN PKSLSLRTHS QTSGWSLTAQ DVFNNVGRTC IEAMAATQGH TQSLHTNALD
EAIALPTDFS ARIARNTQLL LQQESGTTYT IDPWAGSYYV EKLTHDLAQR AWAHIEEAEA
AGGMAAAIEQ GIPKMRIEEA AARTQARIDS GAQKVIGVNT YRLPAEDPLE VLKVDNDDVY
RQQVAKLERL RAERHQGDVD AALEALTRSA DTGEGNLLEL AVDAARHKAT VGEISDALEK
VYGRHQAVIR TISGVYRDEA QEAGDTLLGQ VRTATDEFAD AEGRRPRILV AKMGQDGHDR
GQKVVVSAFA DMGFDVDVGP LFSTPEEVAQ QAIDADVHIV GVSSLAAGHL ALLPALKEAL
AEHGREDIMV VIGGVIPPDD VPILKDMGAA AVFLPGTVIA ESALDLLAKL REQLGH
//
