ID A0A0Q1H510_9FLAO Unreviewed; 688 AA.
AC A0A0Q1H510;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-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=AAY42_00730 {ECO:0000313|EMBL:KQC28592.1};
OS Allomuricauda eckloniae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=346185 {ECO:0000313|EMBL:KQC28592.1, ECO:0000313|Proteomes:UP000050827};
RN [1] {ECO:0000313|EMBL:KQC28592.1, ECO:0000313|Proteomes:UP000050827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK169 {ECO:0000313|EMBL:KQC28592.1,
RC ECO:0000313|Proteomes:UP000050827};
RA Kwon Y.M., Kim S.-J.;
RT "Complete genome of flavobacterium.";
RL Submitted (APR-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:KQC28592.1}.
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DR EMBL; LCTZ01000002; KQC28592.1; -; Genomic_DNA.
DR RefSeq; WP_055392106.1; NZ_LCTZ01000002.1.
DR AlphaFoldDB; A0A0Q1H510; -.
DR STRING; 346185.AAY42_00730; -.
DR PATRIC; fig|1547436.3.peg.145; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000050827; 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.
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, ECO:0000313|EMBL:KQC28592.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000050827}.
FT DOMAIN 561..688
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 688 AA; 76090 MW; C620E8E698C99A8A CRC64;
MSRKNLQNLT LSSTKKLSEV EPPMNFAAGI SPFLRGPYST MYVRRPWTIR QYAGFSTAEE
SNAFYRRNLE AGQKGLSVAF DLPTHRGYDS DNERVVGDVG KAGVAIDSVE DMKVLFDGIP
LDKMSVSMTM NGAVLPIMAF YIAAAEEQGV SMEQLSGTIQ NDILKEFMVR NTYIYPPAPS
MQLVADIFEF TSKNMPKFNS ISISGYHMHE AGAPAALELA YTLSDGIEYI RTGLKAGLKI
DDFAPRLSFF WGIGMDHFTE IAKMRAGRML WAKLVKEFNP KNEKSLMLRT HSQTSGWSLT
EQDPFNNVAR TTIEAMAAVF GGTQSLHTNA LDEAIALPTD FSARIARNTQ IYLQQETHIT
KTVDPWAGSQ VVEKLTEQIA DEAWELIKEI EELGGMTKAI EAGIPKMRIE EAAAKKQARI
DSGQDTIVGV NKYRLEDEDD LQILEVDNAK VRKQQIAQLQ QIKTTRDEDL VQKALGKISV
ASKKVMENDT KRENLLALAV EAAKARATLG EISDAMEEAF GRYRAKIQSV TGVYSKEIKN
NESFENAKKM ADDFALEEGR RPRIMIAKMG QDGHDRGAKV VATGYADLGF DVDIGPLFQT
PSEVAKQAVE NDVHVLGISS LAGGHKTLVP EVIQELKNYG RDDIMVIVGG VIPKQDYDYL
LEHGAIAVFG PGTKISDTAI EILKILMD
//
