ID A0A0F5JNN3_9BACT Unreviewed; 715 AA.
AC A0A0F5JNN3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=HMPREF1536_00941 {ECO:0000313|EMBL:KKB59393.1};
OS Parabacteroides gordonii MS-1 = DSM 23371.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=1203610 {ECO:0000313|EMBL:KKB59393.1, ECO:0000313|Proteomes:UP000033035};
RN [1] {ECO:0000313|EMBL:KKB59393.1, ECO:0000313|Proteomes:UP000033035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS-1 {ECO:0000313|EMBL:KKB59393.1,
RC ECO:0000313|Proteomes:UP000033035};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Martens E., Sakamoto M.,
RA Benno Y., Suzuki N., Matsunaga N., Koshihara K., Seki M., Komiya H.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Parabacteroides gordonii DSM 23371.";
RL Submitted (APR-2013) 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:KKB59393.1}.
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DR EMBL; AQHW01000005; KKB59393.1; -; Genomic_DNA.
DR RefSeq; WP_028726883.1; NZ_KQ033919.1.
DR AlphaFoldDB; A0A0F5JNN3; -.
DR STRING; 1203610.HMPREF1536_00941; -.
DR PATRIC; fig|1203610.3.peg.966; -.
DR HOGENOM; CLU_009523_3_1_10; -.
DR Proteomes; UP000033035; 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 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:UP000033035}.
FT DOMAIN 587..715
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 715 AA; 78314 MW; 19AFA4ACA794B56A CRC64;
MRPNFKNIDI KNAGFAATNA AEWAKANGIE ANWKTPEHIE VKPVYTKEDL EGMEHLHYAS
GLPPYLRGPY SGMYAMRPWT IRQYAGFSTA EESNAFYRRN LASGQKGLSV AFDLPTHRGY
DADNERVVGD VGKAGVSICS LENMKVLFAG IPLNKMSVSM TMNGGVLPVL AFYINAGLEQ
GAKLEEMAGT IQNDILKEFM VRNTYIYPPE FSMKIIADIF EYTSQKMPKF NSISISGYHM
QEAGATADIE MAYTLCDGME YLRAGVNAGI DVDAFAPRLS FFWAIGVNHF MEIAKMRAAR
MLWAKIVKSF GAKNPKSLAL RTHCQTSGWS LTEQDPFNNV GRTCIEAMAA ALGHTQSLHT
NALDEAIALP TDFSARIARN TQIYIQEETK ICKEIDPWAG SYYVESLTNE LVHKGWALIQ
EIESMGGMAK AIETGLPKMR IEEAAARTQA RIDSGVQTIV GVNKYRLPKE DPIDILEIDN
TAVRNEQIAN LKVLRENRDE AAVQKALADI TECVKTKKGN LLELAVKAAG LRASLGEISD
ACEVVVGRYK AIIRTISGVY SSETKKDADF VKACELTEKF AKKEGRQPRI MIAKMGQDGH
DRGAKVVATG YADCGFDVDM GPLFQTPAEA ARQAVENDVH VMGVSSLAAG HKTLVPQVIE
ELKKLGREDI IVIAGGVIPA QDYDFLYKAG VAAIFGPGTS VAKAAVQILE ILLGE
//
