ID A0A1C7P9Z9_9BACT Unreviewed; 713 AA.
AC A0A1C7P9Z9;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-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=PYTT_1455 {ECO:0000313|EMBL:SEH88606.1};
OS Akkermansia glycaniphila.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=1679444 {ECO:0000313|EMBL:SEH88606.1, ECO:0000313|Proteomes:UP000176204};
RN [1] {ECO:0000313|Proteomes:UP000176204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Koehorst J.;
RL Submitted (SEP-2016) 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; LT629973; SEH88606.1; -; Genomic_DNA.
DR RefSeq; WP_067771562.1; NZ_LT629973.1.
DR AlphaFoldDB; A0A1C7P9Z9; -.
DR STRING; 1679444.PYTT_1455; -.
DR KEGG; agl:PYTT_1455; -.
DR PATRIC; fig|1679444.3.peg.1455; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000176204; Chromosome i.
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.
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:UP000176204}.
FT DOMAIN 583..713
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 713 AA; 77799 MW; EE1AADE7C4AA513C CRC64;
MSNIPDFANV AYPETKTGAA APSHASDAWM SNEQIAIDPV YDQAVYGDCK HLGYTAGIAP
FLRGPYATMY VARPWTVRQY AGFSTAEESN AFYRRNLAAG QKGLSIAFDL ATHRGYDSDH
PRVVGDVGKA GVAVDSILDM EILFSGIPLD KMSVSMTMNG AVLPILAFYI VAAEEQGVAQ
ELLTGTIQND ILKEYMVRNT YIYPPDPSMR IIADIFEYTS KNMPKFNSIS ISGYHMQEAG
ATADLEMAYT LADGLQYVRA GIKAGIDIDA FAPRLSFFWA QGKNYFMEVA KMRAARVLWA
KIIKQFNPKN AKSMALRTHS QTSGWSLTEQ DPFNNVARTC IEALAASCGH TQSLHTNALD
EAIALPTDFS ARIARNTQLH LQDETGICKV IDPWGGSYYV EYLTNELIRK GWEHIQEVES
LGGMAKAIET GLPKMRIEEA AARRQAAIDS GSEPIVGVNT QRLEQEAEID ILQVDNDAVR
GAQIARLQKL RAERDGAACE AALEALSKCA ETGEGNLLDM AIKAARARAS LGEISLALEK
HFGRHKAPIK LITGVYGASY GKDPLMDKVR NLTDEFAERE GRRPRILIAK MGQDGHDRGA
KVVSSAYADL GFDVDVGPLF QTPEETAKMA IENDVHIIGM SSLAAGHKVL LPTLIEELKK
QGRPDILVFC GGVIPAQDYG FLREHGAQAI FGPGTNIPAA AEEIMDVLNK HLA
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