ID R7ZPT4_9BACT Unreviewed; 1077 AA.
AC R7ZPT4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Methylmalonyl-CoA mutase {ECO:0000313|EMBL:EON76110.1};
DE EC=5.4.99.2 {ECO:0000313|EMBL:EON76110.1};
GN ORFNames=ADIS_3238 {ECO:0000313|EMBL:EON76110.1};
OS Lunatimonas lonarensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae.
OX NCBI_TaxID=1232681 {ECO:0000313|EMBL:EON76110.1, ECO:0000313|Proteomes:UP000013909};
RN [1] {ECO:0000313|EMBL:EON76110.1, ECO:0000313|Proteomes:UP000013909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK24 {ECO:0000313|EMBL:EON76110.1,
RC ECO:0000313|Proteomes:UP000013909};
RA Singh A.;
RT "A novel strain isolated from Lonar lake, Maharashtra, India.";
RL Submitted (FEB-2013) 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:EON76110.1}.
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DR EMBL; AQHR01000088; EON76110.1; -; Genomic_DNA.
DR AlphaFoldDB; R7ZPT4; -.
DR STRING; 1232681.ADIS_3238; -.
DR PATRIC; fig|1288963.3.peg.3231; -.
DR Proteomes; UP000013909; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.
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; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF01642; MM_CoA_mutase; 2.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR SUPFAM; SSF51703; Cobalamin (vitamin B12)-dependent enzymes; 2.
DR PROSITE; PS51332; B12_BINDING; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00022628};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:EON76110.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013909}.
FT DOMAIN 950..1077
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 1077 AA; 118493 MW; AC0CA45DF63F4FBA CRC64;
MNLLSDSFPP VNKEEWKERM QREGLDLSRT LLEIEEGLAV DSVCTQENAV PLMKDYQNRI
RRFKSNERVW ENVEELDGQS DEELNARIHE SLRDGVDGVL ISLTPSADLS VVFKGVLLAH
VGVWIKFNGS PIVSMRQFAA WIGDQSFDRR QLSGGFLWSK EQLEGVDFRS SEVLELMNFY
LALDRFKCFG IQLSQQHRAS GSLTEVVEVL GFFQDSVGNP PSIEGWSRAF FVHITLESHF
LRQIAILRAM KVLVHQVFLH FGYTVHPSDF YILASSTPEG SDGFHSLIRH TSKALSAIIG
GADGLLLTTY PNTVDGTIGV KRQVTSRIGR ILSEESCLSE VLDPVGGAFL IEKIAWELLD
AVMATIEKRI VGFGWRSLGD LGVLYGDLGE AESSSFLLPE GISCSAVNTP ADLSKFFPIG
SVSGMPPFLR GPYASMYLAR PWTIRQYAGF STAEESNRFY RANLAAGQRG LSIAFDLPTH
RGYDSDHPRV RGDVGKAGVA IDTVEDMKQL FEGIPLEKMS VSMTMNGAVI PIMAFFIVAG
EEQGLTPDQL TGTIQNDILK EFMVRNTYIY PPGPSMRIVS DIFSYTAEKM PRFNSISISG
YHMHEAGAPA DLELAYTLAD GLAYVRKGME AGLQIDDFAP RLSFFWATGM NFFMEIAKLR
AGRVIWARMM SNLGAKNPKS LQLRAHCQTS GWSLTRQDPY NNICRTTSEA MSAVLGHTQS
LHTNSFDEAI ALPTPFSAGI ARETQLFLQQ EAGLTAAIDP FGGSNYLEYL TDRLIMRAEG
HIREVEELGG MEKAIELGIP KMRIEEAAAK KQARIDEGID VIVGVNRYQS TDDEEIDILR
VDNEAVRQSQ VNRIQETKKK RDLNTVENCL NRIEEAAETG VGNLLALAVD AARARATLGE
ISMAMEKSFG RYQATARTIS GAYLSEAGDS KVIQLAKEKA DEFAKLEGRR PRILVAKIGQ
DGHDRGAKII ASGFSDLGFD VDVGPLFQTP EEVAKQAVEN DVHVVGVSSQ AGGHRTLVPE
LIAELHKSGR PDITVVAGGV IPPEDESYLL ECGVKAVFGS GVAVSKAALR VLEVLSE
//