ID C6XJ84_HIRBI Unreviewed; 712 AA.
AC C6XJ84;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN OrderedLocusNames=Hbal_1490 {ECO:0000313|EMBL:ACT59179.1};
OS Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hirschia.
OX NCBI_TaxID=582402 {ECO:0000313|EMBL:ACT59179.1, ECO:0000313|Proteomes:UP000002745};
RN [1] {ECO:0000313|Proteomes:UP000002745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49814 / DSM 5838 / IFAM 1418
RC {ECO:0000313|Proteomes:UP000002745};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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; CP001678; ACT59179.1; -; Genomic_DNA.
DR RefSeq; WP_015827329.1; NC_012982.1.
DR AlphaFoldDB; C6XJ84; -.
DR STRING; 582402.Hbal_1490; -.
DR KEGG; hba:Hbal_1490; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_3_1_5; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000002745; 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: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, ECO:0000313|EMBL:ACT59179.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002745}.
FT DOMAIN 580..712
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 712 AA; 78253 MW; FB70857EB27702A3 CRC64;
MNVPTLEDWY ELGAKELRGR EIDDLNKTTP EGIKIKPVYT KRDVPDSIEK ELPGFEPYTR
GVRATMYANQ PWTIRQYAGF STAEESNAFY RKNLKAGQKG LSVAFDLATH RGYDSDHPRV
AGDVGKAGVA IDTVEDMKIL FDGIPLDEMS VSMTMNGAVI PVLAMFIVAG EEQGVDRSKL
SGTIQNDILK EFMVRNTFIY PPEFSMRIIG DIIEYTSQDM PKYNSISISG YHMQEAGATL
AQELAFTLAD GMEYVREAKK KGLDIDAFAG RLSFFFCIGM NVFMEAAKLR AARQIWSKIM
TNLGAKSERS KMLRTHCQTS GVSLTEQDPY NNVVRTAYEA MAAVLGGTQS LHTNSFDEAI
ALPTETSARI ARNTQLILQY ETGVTDVVDP LGGSFYVEAL TQGLVDQAWD MINEIEAEGG
MTKAIEKGLP KLKIEQAAAK RQARVDKGED VVIGVNKYRL EEEDPINILE IDNAAVRKSQ
ISRINKVKVV RDSQACNSTL EKLKDIAENG NGNILRAAVE CARARATLGE ISNALEDVFG
RHQPITRVIK GVYSDAYKED PIYINIQANI QKYEHEKGTA PRILIAKMGQ DGHDRGAKII
ATAFADLGFG VNMTDLFSTP DEVAELAIIS EVDAIGISSL AAGHKTLVPE LIDVLKKLSR
DDIKIFVGGV IPEQDYSFLK EAGVIDIFGP GTNVLDAAYS VFAAISGKSR NT
//
