ID H5SB05_9BACT Unreviewed; 654 AA.
AC H5SB05;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=HGMM_F06F04C22 {ECO:0000313|EMBL:BAL53341.1};
OS uncultured Bacteroidetes bacterium.
OC Bacteria; Bacteroidota; environmental samples.
OX NCBI_TaxID=152509 {ECO:0000313|EMBL:BAL53341.1};
RN [1] {ECO:0000313|EMBL:BAL53341.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT "Genetic and functional properties of uncultivated thermophilic
RT crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT genome fragments.";
RL Environ. Microbiol. 7:1967-1984(2005).
RN [2] {ECO:0000313|EMBL:BAL53341.1}
RP NUCLEOTIDE SEQUENCE.
RA Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S.,
RA Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.;
RT "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA
RT Pathway Dominates a Subsurface Ecosystem.";
RL PLoS ONE 7:e30559-e30559(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; AP011655; BAL53341.1; -; Genomic_DNA.
DR AlphaFoldDB; H5SB05; -.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 516..648
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT COILED 422..456
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 654 AA; 71037 MW; 4B9476D4C6186050 CRC64;
MYANRPWTIR QYAGFSTAEE SNAFYRQALA QGQTGLSIAF DLATHRGYDS DNPRVVGDVG
KAGVAIDTVE DMKILFDGID LGKVSVSMTM NGAVLPIMAM FIVAAEEQGV EQSALSGTIQ
NDILKEFLVR NTYIYPPEPS MRIVADIIAY TSKHMPRFNS ISISGYHMHE AGATAVQELA
FTLADGLEYV RAAISRGLDV DQFAPRLSFF FGIGLNFFME IAKLRAARLL WAQLMKERFS
PSNAASMMLR THCQTSGWSL TAQDPYNNII RTTIEALAAV LGGTQSLHTN SFDEALALPS
EFSARIARNT QLILAEETNI CRVVDPLGGS YYVESLTASL ARHARALIEE IESQGGMVAA
IASGYAKALI EEAAARRQAA IDRGEEVIVG VNKYRPPSEP PVEILEVDNT KVRAQQIARL
ERVKATRDAN AVAAALERLE QAARNDKENL LTYAIEAARV RATVGEISQA LANVFGRYQT
VSTAITGIYC ASYHGDASFE ALCQRVRRFE EATGRRPRIL VAKLGQDGHD RGLKVIASGF
ADLGFDVDLG PLFQTPEEVA RQAIENDVHV VGISSQAGAH KALIPELIER LRAEGAGDIL
VVAGGIIPPK DYDDLHRAGV HAIFGPGTPV LDAAEAVLDL LEHHWNVENA AASH
//
