ID A0A0U4C598_9BACT Unreviewed; 712 AA.
AC A0A0U4C598;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=AUC43_10190 {ECO:0000313|EMBL:ALW85432.1};
OS Hymenobacter sedentarius.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1411621 {ECO:0000313|EMBL:ALW85432.1, ECO:0000313|Proteomes:UP000059542};
RN [1] {ECO:0000313|EMBL:ALW85432.1, ECO:0000313|Proteomes:UP000059542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5B {ECO:0000313|EMBL:ALW85432.1,
RC ECO:0000313|Proteomes:UP000059542};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-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}.
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DR EMBL; CP013909; ALW85432.1; -; Genomic_DNA.
DR RefSeq; WP_068192689.1; NZ_CP013909.1.
DR AlphaFoldDB; A0A0U4C598; -.
DR STRING; 1411621.AUC43_10190; -.
DR KEGG; hyg:AUC43_10190; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000059542; 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:UP000059542}.
FT DOMAIN 582..712
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 712 AA; 76476 MW; 9B7402BB44E7711B CRC64;
MKPDFSTIPY DAAPAPSAAP VAAETAATLT PEGIALKPVY TPADVAGLDH LGFGAGQAPY
LRGPYASMYV QNPWTIRQYA GFSTAEASNA FYRRNLAGGQ KGLSVAFDLA THRGYDSDHP
RVQGDVGKAG VAIDSVEDMK ILFDQIPLGE MSVSMTMNGA VLPVLAFYIV AAEEQGVSPD
KLAGTIQNDI LKEFMVRNTY IYPPAPSMRI IADIFSYTAA NMPKFNSISI SGYHMQEAGA
TADLELAYTL ADGLEYVRAG LAAGMKIDEF APRLSFFWAI GMPHFMEIAK LRAGRLLWAK
LMQQFNPTNP KSLALRTHCQ TSGYSLTEQD PYNNVARTAI EALAAVLGGT QSLHTNALDE
AIALPTDFSA RIARNTQLYL QHETDITKVV DPWGGSYYVE TLTHELADKA WVLIQEVEEL
GGMAKAIETG LPKLRIEEAA ARKQARIDSG KEVIVGVNKY KTTEKTEVEV LDIDNDAVRT
SQIERLNQIR ATRDTAAVQA ALAALTEAAQ TGANNLLALA VDAARVRATL GEISDALEVA
YGRHQATTRT VTGVYSSEMD YDQEFAKARA AAEEFAAREG RRPRMLVAKM GQDGHDRGAK
IIATSFADVG FDVDIAPLFQ TPAEVARQAA DNDVHVVGVS SLAAGHKTLL PQLLTELKQL
GREDILVIAG GVIPAQDYPF LYAAGVAGVY GPGTVIATAA QEILGKLGAQ SE
//
