ID E1X0H3_HALMS Unreviewed; 709 AA.
AC E1X0H3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN Name=mutB {ECO:0000313|EMBL:CBW27999.1};
GN OrderedLocusNames=BMS_3249 {ECO:0000313|EMBL:CBW27999.1};
OS Halobacteriovorax marinus (strain ATCC BAA-682 / DSM 15412 / SJ)
OS (Bacteriovorax marinus).
OC Bacteria; Bdellovibrionota; Bacteriovoracia; Bacteriovoracales;
OC Halobacteriovoraceae; Halobacteriovorax.
OX NCBI_TaxID=862908 {ECO:0000313|EMBL:CBW27999.1, ECO:0000313|Proteomes:UP000008963};
RN [1] {ECO:0000313|Proteomes:UP000008963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-682 / DSM 15412 / SJ
RC {ECO:0000313|Proteomes:UP000008963};
RX PubMed=22955231; DOI=10.1038/ismej.2012.90;
RA Crossman L.C., Chen H., Cerdeno-Tarraga A.M., Brooks K., Quail M.A.,
RA Pineiro S.A., Hobley L., Sockett R.E., Bentley S.D., Parkhill J.,
RA Williams H.N., Stine O.C.;
RT "A small predatory core genome in the divergent marine Bacteriovorax
RT marinus SJ and the terrestrial Bdellovibrio bacteriovorus.";
RL ISME J. 7:148-160(2013).
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; FQ312005; CBW27999.1; -; Genomic_DNA.
DR RefSeq; WP_014245769.1; NC_016620.1.
DR AlphaFoldDB; E1X0H3; -.
DR STRING; 862908.BMS_3249; -.
DR KEGG; bmx:BMS_3249; -.
DR PATRIC; fig|862908.3.peg.3105; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_3_1_7; -.
DR Proteomes; UP000008963; 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: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:UP000008963}.
FT DOMAIN 579..709
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 709 AA; 77831 MW; 15AB837115CE4E96 CRC64;
MKSINDWKEL ATKEQKGKSP ESLITKSAEG IDIKPLYTKE DISSFDNTNT LPGFAPFIRG
PRATMYTGRP WTIRQYAGFS TAEESNAFYR KALAAGGQGV SVAFDLATHR GYDSDHPRVS
GDVGKAGVAI DSVEDMKVLF DSIPLDKVSV SMTMNGAVLP ILANYIIAAE EQGVSKDKLS
GTIQNDILKE FMVRNTYIYP PAPSMKAIAD IFEYTSKNMP KFNSISISGY HIQEAGADNA
LELAYTLADG REYIETAIAA GMNIDDFAPR LSFFFGIGMN FYMEIAKLRA ARMLWAEIVS
EYEPKNVKST MLRTHCQTSG WSLTEQDPYN NVIRTTVEAM AAVFGGTQSL HTNALDEAVA
LPTEFSARIA RNTQIILQEE TGITNVVDPW GGSYMMETLT NEIADRAREL MKEVHKLGGM
AKAIESGVPK LKIEEAAAIK QAKIDRGEYT IVGVNKYKVE NEEEIEILEI DNTAVRESQI
KRLAQLKKDR DNEEVNKALS ALTEYAKTGI GNGLELAVNA ARVRCTVGEI SDALEKHWGR
YNANSATVSG VYGSAYEEDE NWNMIKERIE KFEKENGRRP RMLVAKMGQD GHDRGAKVIA
TAYADVGFDI DLAPLFSTPA EVAKQAVEND VHVIGVSSLA AGHKTLIPDL INELKKLGGE
DIVVVAGGVI PKQDYDFLYN SGVKGIYGPG TAIPYAAEDV LNHIENSKK
//
