ID A0A0F7K0U1_9GAMM Unreviewed; 716 AA.
AC A0A0F7K0U1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=AAY24_13530 {ECO:0000313|EMBL:AKH21214.1};
OS Sedimenticola thiotaurini.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Sedimenticola.
OX NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH21214.1, ECO:0000313|Proteomes:UP000034410};
RN [1] {ECO:0000313|EMBL:AKH21214.1, ECO:0000313|Proteomes:UP000034410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH21214.1,
RC ECO:0000313|Proteomes:UP000034410};
RX PubMed=26089430;
RA Flood B.E., Jones D.S., Bailey J.V.;
RT "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1, a
RT Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur-Oxidizing
RT Gammaproteobacterium Isolated from Salt Marsh Sediments.";
RL Genome Announc. 3:e00671-15(2015).
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; CP011412; AKH21214.1; -; Genomic_DNA.
DR RefSeq; WP_046860143.1; NZ_CP011412.1.
DR AlphaFoldDB; A0A0F7K0U1; -.
DR KEGG; seds:AAY24_13530; -.
DR PATRIC; fig|1543721.4.peg.2803; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000034410; 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: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:AKH21214.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000034410}.
FT DOMAIN 585..716
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 716 AA; 77883 MW; D1D1E7C932BA8F87 CRC64;
MANKPKPTLE EWKKQAEKEL RGRPLEALNW QTPEGIGIKP LYTAADLAGL EHVDSLPGFA
PYMRGPRATM YAGRPWTVRQ YAGFSTAEES NAFYKRNLAA GQQGLSVAFD LATHRGYDSD
HPRVVGDVGK AGVAIDSVED MKILFDSIPL DKVSVSMTMN GAVLPVMASY IVAAEEQGVP
PEKLAGTLQN DILKEFMVRN TYIYPPEPSM RIVADIIGYT AEHMPKFNSI SISGYHMQEA
GSTLVQELAF TIADGLEYVR AALAKGLDVD QFAPRLSFFF AIGMNFFMEA AKLRAARLLW
SELMEKHFQP KDERSKMLRT HCQTSGVSLT AKDPYNNIMR TTIEAMAAVL GGTQSLHTNA
FDEALALPTD NSARIARNTQ LVIQEETGIT KVVDPLAGSY YVESLTNAMV EEARKLIDEV
EALGGMTKAV ESGMPKLRIE EAAALRQARI DRGEEVIVGV NKYQLEEEPE IDVLDIDNTA
VREAQVARLQ RIRAERDATA HKAALDALVA AAKDGSGNLL ELAVDAARAR ATVGEISDAL
ESVYNRHKAI TRSVSGVYGS AYDGDDAFDK IKQEIARFAE EQGRRPRMLV VKMGQDGHDR
GAKVIATAYA DLGFDVDIGP MFQTPEEAAR QAAENDVHVV GVSSLAAGHK TLVPALLQAL
KDEGAEDILV VCGGVIPPQD YPALLEMGVA AVYGPGTNIP ASAAEMLAFI RRRQGI
//
