ID A0A2T0ZY55_9ACTN Unreviewed; 725 AA.
AC A0A2T0ZY55;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=CLV47_11010 {ECO:0000313|EMBL:PRZ41285.1};
OS Antricoccus suffuscus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Antricoccaceae; Antricoccus.
OX NCBI_TaxID=1629062 {ECO:0000313|EMBL:PRZ41285.1, ECO:0000313|Proteomes:UP000237752};
RN [1] {ECO:0000313|EMBL:PRZ41285.1, ECO:0000313|Proteomes:UP000237752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100065 {ECO:0000313|EMBL:PRZ41285.1,
RC ECO:0000313|Proteomes:UP000237752};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
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 -!- 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:PRZ41285.1}.
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DR EMBL; PVUE01000010; PRZ41285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0ZY55; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000237752; 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:UP000237752}.
FT DOMAIN 591..723
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 725 AA; 78077 MW; C96359DFE8260CA8 CRC64;
MTVRNFADVP YDAEPDGAKI DAVKANESST WAAPEGIGVK NVYTPADLDG LKNLDTYPGL
DPFIRGPYPT MYNSQPWTVR QYAGFSTAEE SNAFYRRNLA AGQKGLSVAF DLATHRGYDS
DHPRVAGDVG MAGVAIDSIY DMRQLFDGIP LDEMSVSMTM NGAVLPILAL YVVAAEEQGV
PPEKLAGTIQ NDILKEFMVR NTYIYPPLPS MRIISDIFAY TAAKMPKFNS ISISGYHIQE
AGATNDLELA YTLADGLEYL RTGVAAGLDI DKFAPRLSFF WAIGMNYFME VAKMRAGRAI
WSQIMQQFDP KNPKSKSLRT HSQTSGWSLT AQDVYNNVAR TCIEAMAATA GHTQSLHTNA
LDEALALPTD FSARIARNTQ LVLQQEAGAG DIIDPWGGSY YVERLTEELI ERAWAHIEEV
EAAGGMAKAI EAGIPKMRIE EAAARTQARI DSGKQVVVGI NTFVPTKDDG VDVLKIDNAS
VRKQQLAKLE RLRAERDDTE VKRTLDALTK AAGVQAKGTE MGTNLLALAI DAARAKATVG
EISDALEEVF GRHTAVIRTI SGVYKKEAGD AKNVEAVLAA ADKFADEEGR RPRILVAKMG
QDGHDRGQKV IVSAFADMGF DVDVGPLFST PEEVARQAID ADVHIVGVSS LAAGHLTLVP
ALRDELAKQG RPDIVIVVGG VIPPADVPTL LDMGAAAVFP PGTVIADSAL KLLDGLSKNL
GHPAA
//
