ID A0A0P7WJN9_9RHOB Unreviewed; 666 AA.
AC A0A0P7WJN9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=(2R)-ethylmalonyl-CoA mutase {ECO:0000313|EMBL:KPP87426.1};
GN Name=ecm {ECO:0000313|EMBL:KPP87426.1};
GN ORFNames=HLUCCO07_10290 {ECO:0000313|EMBL:KPP87426.1};
OS Rhodobacteraceae bacterium HLUCCO07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666914 {ECO:0000313|EMBL:KPP87426.1, ECO:0000313|Proteomes:UP000050369};
RN [1] {ECO:0000313|EMBL:KPP87426.1, ECO:0000313|Proteomes:UP000050369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCO07 {ECO:0000313|EMBL:KPP87426.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) 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}.
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:KPP87426.1}.
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DR EMBL; LJSU01000010; KPP87426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7WJN9; -.
DR STRING; 1666914.HLUCCO07_10290; -.
DR PATRIC; fig|1666914.4.peg.35; -.
DR Proteomes; UP000050369; 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:InterPro.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 532..661
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 666 AA; 73090 MW; 48838DEBB41E17E0 CRC64;
MSQTQEDRQT SRSDRQADRP WLIRTYSGHS TAKASNALYR GNLAKGQTGL SVAFDLPTQT
GYDSDHVLAR GEVGKVGVPI CHLGDMRTLF DQIPLDQMNT SMTINATAPW LLALYIAVAE
EQGADVTKLQ GTVQNDIIKE YLSRGTYVCP PKPSLKLIGD VAEYCYANVP KWNPMNVCSY
HLQEAGATPE QELAFALATA IAVLDELKPR VPPEDFPALC GRISFFVNAG IRFVTEMCKM
RAFVDLWDEI LLDRYGVENP KFRRFRYGVQ VNSLGLTEQQ PENNVYRILI EMLAVTLSKK
ARARAVQLPA WNEALGLPRP WDQQWSMRMQ QIMAYETDLL EYDDLFDNNP AVDARVAALK
EGARHELETL DGMGGAVAAI EYMKARLVDS NAERLNRIEA GETVVVGVNK WIEGEPSPLT
SGEGGILTVD PAVEAEQIER LDDWRASRDS TAVDRALADL RAAATSGANI MEPSITAAKA
GVTTGEWAEV MREVFGEYRG PTGVSRAVSN KTEGLDDIRA AVDTVSDRLG RRLKFLVGKP
GLDGHSNGAE QIAFRARDCG MDIEYEGIRL TPEEIVEAAK ESAAHVIGLS ILSGSHMPLV
EDTLNRLRDA GLGHVPVIVG GIIPAEDAKT LRDLGVAQVY TPKDFELNTI MMDIVSLADP
KEIAAE
//
