ID A0A2Z2NWA1_9GAMM Unreviewed; 711 AA.
AC A0A2Z2NWA1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN Name=scpA_1 {ECO:0000313|EMBL:ASJ73988.1};
GN ORFNames=IMCC3135_19545 {ECO:0000313|EMBL:ASJ73988.1};
OS Granulosicoccus antarcticus IMCC3135.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Granulosicoccaceae; Granulosicoccus.
OX NCBI_TaxID=1192854 {ECO:0000313|EMBL:ASJ73988.1, ECO:0000313|Proteomes:UP000250079};
RN [1] {ECO:0000313|EMBL:ASJ73988.1, ECO:0000313|Proteomes:UP000250079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC3135 {ECO:0000313|EMBL:ASJ73988.1,
RC ECO:0000313|Proteomes:UP000250079};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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; CP018632; ASJ73988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z2NWA1; -.
DR KEGG; gai:IMCC3135_19545; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000250079; 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:ASJ73988.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000250079}.
FT DOMAIN 579..711
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 711 AA; 77660 MW; 1C31236DE5F99C59 CRC64;
MSESNSTWTE LARRELKDRP LESICTQTPE GISIKPLYTI EDSPAAAAEA IPGVAPFARG
VRATMYTGRP WTIRQYAGFS TAEASNAFYR KNLAAGQKGL SVAFDLATHR GYDSDHERVV
GDVGKAGVAI DTVEDMKILF DGIPLDKMSV SMTMNGAVLP ILAMFIVAGE EQGYDQSLLS
GTVQNDVLKE FMVRNTYIYP PEPSMRIVAD IIDYTSREMP RFNSISISGY HMQEAGANLA
QELAYTLADG MEYVRAAQSK GLDIDAFAGR LSFFFCIGMD FFMEVAKLRA ARMLWSRIMT
DLGAQKESSK LLRTHCQTSG VSLTEQDPYN NVVRTAYEAL AAVLGGTQSL HTNSFDEAIA
LPTEASARIA RNTQLILQHE TGVTRTVDPL GGSYYVESLT SELMETAWAM IQEIEEHGGM
TKALLDGLPK RRIEEAATAR QARVDNGDDV IVGVNQYRLE NEVPIDVHRV DNAEVRRQQI
ERLKRVRRER DEAICAKSLA DLTQIAKSQS GNLLAAAVDA ARNRATLGEI SDALESEFGR
HQAKTEVVSG IYQKQSETSP EFLHVKKRVE DFKTSHGRAP HLLVAKMGQD GHDRGAKVIA
SSFGDIGFKI GMSDLFLTPE EVADLCIKDG VDVVGVSSLA GGHQTLIPQL INLLADKGRA
DIKVVCGGVI PEQDYEALRD AGVAEIFGPG TSVIDAANAV LGQILGERRN R
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