ID A0A173XXB9_9BACE Unreviewed; 715 AA.
AC A0A173XXB9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:CUN56591.1};
GN Synonyms=scpA {ECO:0000313|EMBL:KAA5233181.1};
GN ORFNames=ERS852397_00454 {ECO:0000313|EMBL:CUN56591.1}, F2Z22_00750
GN {ECO:0000313|EMBL:KAA5233181.1};
OS Bacteroides finegoldii.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=338188 {ECO:0000313|EMBL:CUN56591.1, ECO:0000313|Proteomes:UP000095517};
RN [1] {ECO:0000313|EMBL:CUN56591.1, ECO:0000313|Proteomes:UP000095517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608840 {ECO:0000313|EMBL:CUN56591.1,
RC ECO:0000313|Proteomes:UP000095517};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAA5233181.1, ECO:0000313|Proteomes:UP000421791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A6 {ECO:0000313|EMBL:KAA5233181.1,
RC ECO:0000313|Proteomes:UP000421791};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
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; CYZH01000002; CUN56591.1; -; Genomic_DNA.
DR EMBL; VWAK01000001; KAA5233181.1; -; Genomic_DNA.
DR RefSeq; WP_007751753.1; NZ_VWAO01000002.1.
DR AlphaFoldDB; A0A173XXB9; -.
DR STRING; 338188.ERS852397_00454; -.
DR GeneID; 61620907; -.
DR Proteomes; UP000095517; Unassembled WGS sequence.
DR Proteomes; UP000421791; 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: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.
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, ECO:0000313|EMBL:CUN56591.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000095517}.
FT DOMAIN 586..715
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 715 AA; 78727 MW; 68A1A9EE3091C651 CRC64;
MRKDFKNIDI YAAFQPANGA EWQKANGISA DWKTPEHIEV KPVYTKEDLE GMEHLGYAAG
LPPYLRGPYS VMYTLRPWTI RQYAGFSTAE ESNAFYRRNL ASGQKGLSVA FDLATHRGYD
PDHERVVGDV GKAGVSICSL ENMKVLFDGI PLNKMSVSMT MNGAVLPVMA FYINAGLEQG
AKLEEMAGTI QNDILKEFMV RNTYIYPPAF SMKIISDIFE YTSQKMPKFN SISISGYHMQ
EAGATADIEL AYTLADGLEY LRAGTAAGID IDAFAPRLSF FWAIGTNHFM EIAKMRAARM
LWAKIVKQFN PKNPKSLALR THSQTSGWSL TEQDPFNNVG RTCIEAMAAA LGHTQSLHTN
ALDEAIALPT DFSARIARNT QIYIQEETYI CKNVDPWGGS YYVETLTNEL AHKAWEHIQE
IEKLGGMAKA IETGIPKMRI EEAAARTQAR IDSGQQTIVG VNKYRLDKEA PIDILEIDNT
AVRLEQIENL KRLKEGRNQA EVDKALAAIT ECVKTGKGNL LELAVEAARV RATLGEISSA
CEQVVGRYKA IIRTISGVYS SESKNDSDFK RACELAEKFA KKEGRQPRIM IAKMGQDGHD
RGAKVVATGY ADCGFDVDMG PLFQTPAEAA REAVENDVHV VGVSSLAAGH KTLVPQIIEE
LKKLGREDIV VIAGGVIPAQ DYDFLYKAGV AAIFGPGTPV AKAACQILEI LMDEE
//
