ID I0AMD8_IGNAJ Unreviewed; 723 AA.
AC I0AMD8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN OrderedLocusNames=IALB_2442 {ECO:0000313|EMBL:AFH50145.1};
OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS Mat9-16).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Ignavibacteriaceae; Ignavibacterium.
OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH50145.1, ECO:0000313|Proteomes:UP000007394};
RN [1] {ECO:0000313|EMBL:AFH50145.1, ECO:0000313|Proteomes:UP000007394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC {ECO:0000313|Proteomes:UP000007394};
RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA Bryant D.A.;
RT "Complete genome of Ignavibacterium album, a metabolically versatile,
RT flagellated, facultative anaerobe from the phylum Chlorobi.";
RL Front. Microbiol. 3:185-185(2012).
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; CP003418; AFH50145.1; -; Genomic_DNA.
DR RefSeq; WP_014561287.1; NC_017464.1.
DR AlphaFoldDB; I0AMD8; -.
DR STRING; 945713.IALB_2442; -.
DR GeneID; 78244030; -.
DR KEGG; ial:IALB_2442; -.
DR PATRIC; fig|945713.3.peg.2450; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_3_1_10; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000007394; 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.
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:UP000007394}.
FT DOMAIN 594..723
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 723 AA; 81258 MW; A5CE44C3F2319DA9 CRC64;
MKPNFKEIKL DLTVKQISKT EWKEKFKQET GKTVEDFIWE TMEKIPVKPL YTQEDIKELE
HTDYLSGLPP FLRGPYSTMY VQRPWTVRQY AGFSTAEESN AFYRRNLAQG QMGLSVAFDL
ATHRGYDSDH PRVVGDVGKA GVAIDTVEDM KILFDQIPLD KMSVSMTMNG AVIPVMAFYI
VAAEEQGVKH EQLTGTIQND ILKEYMVRNT YIYPPEMSMR IIADIFKFTA KNMPKFNSIS
ISGYHMQEAG ATADLEMAYT LADGLEYVRT GIKAGMDIDE FAPRLSFFWA EGMNYFMEVA
KLRAARLIWA KIIKQFNPKN PKSMSLRTHS QTSGWSLSEQ DPFNNVVRTC IEALAAALGH
TQSLHTNSLD EAIALPTDFS ARIARNTQLY LQDETLITKV IDPWGGSYYV EALTDALLQK
GWQHILEVES YGGMTKAIEA GIPKMRIEEA AARRQARIDS GKETIVGVNK FRLEKEEPIE
ILEVDNTAVR QNQIKRIQEV KQKRNETEVL HALDAITKAA QSGEGNLLEL AIDAARKRAT
LGEISYAIEK VCGRYQAVTR TISGVYSSEY SKDDQLFNEV RKLTDEFAQR EGRRPRIMIA
KMGQDGHDRG AKVVATAYAD MGFDVDVGPL FQTPEETAKQ AVENDVHVVG MSSLAGGHKT
LLPQLVDELK KLGREDIIVI CGGVIPVQDY DYLYEHGASA IFGPGTKIPE AGKKIMELIN
ERF
//
