ID G8R8Q7_OWEHD Unreviewed; 709 AA.
AC G8R8Q7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN OrderedLocusNames=Oweho_1496 {ECO:0000313|EMBL:AEV32487.1};
OS Owenweeksia hongkongensis (strain DSM 17368 / CIP 108786 / JCM 12287 / NRRL
OS B-23963 / UST20020801).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Owenweeksiaceae;
OC Owenweeksia.
OX NCBI_TaxID=926562 {ECO:0000313|EMBL:AEV32487.1, ECO:0000313|Proteomes:UP000005631};
RN [1] {ECO:0000313|EMBL:AEV32487.1, ECO:0000313|Proteomes:UP000005631}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 17368 / JCM 12287 / NRRL B-23963
RC {ECO:0000313|Proteomes:UP000005631};
RX PubMed=23450211; DOI=10.4056/sigs.3296896;
RA Riedel T., Held B., Nolan M., Lucas S., Lapidus A., Tice H., Del Rio T.G.,
RA Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S., Liolios K.,
RA Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Rohde M., Tindall B.J., Detter J.C., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Genome sequence of the orange-pigmented seawater bacterium Owenweeksia
RT hongkongensis type strain (UST20020801(T)).";
RL Stand. Genomic Sci. 7:120-130(2012).
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; CP003156; AEV32487.1; -; Genomic_DNA.
DR RefSeq; WP_014201843.1; NC_016599.1.
DR AlphaFoldDB; G8R8Q7; -.
DR STRING; 926562.Oweho_1496; -.
DR KEGG; oho:Oweho_1496; -.
DR PATRIC; fig|926562.3.peg.1499; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_3_1_10; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000005631; 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:UP000005631}.
FT DOMAIN 579..709
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 709 AA; 78521 MW; 20B7CA099FF42878 CRC64;
MKRHDFQNTN YSKSQAQETK SSATWNTPEE IKVPNQFSKV DFGKLTHLDY VAGLPPYLRG
PYSTMYVSRP WTIRQYAGFS TAEESNAFYR RNLAAGQKGL SVAFDLATHR GYDSDHERVV
GDVGKAGVAI DSVEDMKILF DQIPLDEMSV SMTMNGAVIP IMAFYIVAAE EQGVSPEKLS
GTIQNDILKE FMVRNTYIYP PLPSMRIVAD IFEYTKNNMP RFNSISISGY HMHEAGATAD
IELAYTLADG MEYIRTGMQA GLDIDDFAPR LSFFWGIGMN HFMEIAKMRA ARMLWAKIVK
SLGAKNPKSM ALRTHSQTSG YSLTEQDPFN NVARTTIEAM AAVFGGTQSL HTNSLDEAIA
LPTDFSARIA RNTQLIIQEE LGVTRTVDPW GGSYYVEYLT DQLVEKAWKL IEEVEELGGM
AKAIETGVPK MRIEEAAAKK QARIDSGKEW IIGVNAYKNE KDEEIELLEV DNAVVRQKQI
ERLESIRSTR DQQKVDANLK AITEAAKSGE GNLLALAVEA ARHRATLGEI SLAMEKAFDR
YTATIRSISG VYSNEMKKDE KFEKAQQLAD KFEAVEGRRP RIMIAKMGQD GHDRGAKVVA
TSFADLGFDV DIGPLFQTPA EAAKQAIEND VHLLGVSSLA AGHKTLVPQV IDELKKQGRE
DILVIAGGVI PQNDYKYLFE AGVVGVFGPG TVIAEAAARI LEVMIEGRN
//
