ID A0A136N442_9BACT Unreviewed; 690 AA.
AC A0A136N442;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=UZ09_BCD002000103 {ECO:0000313|EMBL:KXK40940.1};
OS Bacteroidetes bacterium OLB9.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1617420 {ECO:0000313|EMBL:KXK40940.1, ECO:0000313|Proteomes:UP000070267};
RN [1] {ECO:0000313|EMBL:KXK40940.1, ECO:0000313|Proteomes:UP000070267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB9 {ECO:0000313|EMBL:KXK40940.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXK40940.1}.
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DR EMBL; LNBW01000003; KXK40940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136N442; -.
DR STRING; 1617420.UZ09_BCD002000103; -.
DR PATRIC; fig|1617420.3.peg.111; -.
DR Proteomes; UP000070267; 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.
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:KXK40940.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 560..690
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 690 AA; 75415 MW; EF201E1DD5D133B4 CRC64;
MNTQNNPATP EGIQLKKRYV LEDLKTCRHL GFQSGTPPFL RGPYSTMYVV SPWTIRQYSG
FSTAKDSNAF YRRNLAAGQK GLSVAFDLAT HRGYDSDHPR VAGDVGMAGV AIDTVEDMKV
LFDGIPLDEM SVSMTMNGAV IPVMAFFIIA AEEQGVSMEK LTGTIQNDIL KEFMVRNTYI
YPPGPSMRII SDIFRFTAVH MPKFNSISIS GYHMHEAGAP ADLELAYTIA DGMEYIRAGQ
KAGLDIDEFV SRFSFLGHRY EFFMEIAKMR AGRLLWAKIV KEFGAKSDKS MALRTHCQTS
GYSLTAQDPY NNIARTCIEA LSAVFGGTQS LHTNSLDEAI ALPTDASAKI ARDTQKYLQS
ETRITSAIDP MGGSYYVESL TADLADKAWE HICEVEALGG MAAAIEAGIP KMRIEEAAAA
KQARIDSRSE LITGVNFNQR NNEPDLDILV VDNTSVRKEQ IDAITKVKAT RDQTAVDTAL
NYITKVAESG EGNLLEAAVN AARIRATLGE ISMAMEKVFG RFTATNKTIT GVYAKEISMN
DKFKEARQLS DQFAELEGRR PRIMVAKLGQ DGHDRGAKVI ATSFADLGFD VDMGPLFQTP
EEAVRQAAEN DVHILGISSL AAGHKTLVPQ TIEALKTIGR EDILVVAGGV IPPQDYQFLF
DAGVAAVFGP GTIIAEAAID ILKIMIDNIR
//
