ID A0A126PCG8_9BACT Unreviewed; 722 AA.
AC A0A126PCG8;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-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=AXW84_16260 {ECO:0000313|EMBL:AMJ66804.1};
OS Hymenobacter sp. PAMC 26628.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1484118 {ECO:0000313|EMBL:AMJ66804.1, ECO:0000313|Proteomes:UP000059956};
RN [1] {ECO:0000313|EMBL:AMJ66804.1, ECO:0000313|Proteomes:UP000059956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC26628 {ECO:0000313|EMBL:AMJ66804.1,
RC ECO:0000313|Proteomes:UP000059956};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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; CP014304; AMJ66804.1; -; Genomic_DNA.
DR RefSeq; WP_068235505.1; NZ_CP014304.1.
DR AlphaFoldDB; A0A126PCG8; -.
DR STRING; 1484118.AXW84_16260; -.
DR KEGG; hyz:AXW84_16260; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000059956; 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.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000059956}.
FT DOMAIN 595..722
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 9..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 722 AA; 77724 MW; 132FE3890D96D78B CRC64;
MKPDFAAIAY DAAPPQPTPG GPEAPAQSTP EGIALKPCYT AADVAHLDHL GFGAGQAPYL
RGPYASMYTQ NPWTVRQYAG FSTAEASNAF YRRNLAGGQK GLSVAFDLAT HRGYDSDHPR
VQGDVGKAGV AIDSVEDMKI LFDQIPLEQM SVSMTMNGAV LPVLAFFIVA AEEQGVPPEK
LTGTIQNDIL KEFMVRNTYI YPPGPSMRII ADIFSYTAAR MPKFNSISIS GYHMQEAGAT
ADLELAYTLA DGLEYVRAGL AVGLPIDDFA PRLSFFWAIG MNHFMEIAKL RAGRLLWAKL
MQQFNPQNPK SLALRTHCQT SGYSLTEQDP YNNVARTAIE ALAAVLGGTQ SLHTNALDEA
IALPTDFSAR IARNTQLYLQ HETDVTKVVD PWGGSYYVET LTHELADRAW ALIQEVEQLG
GMAKAIETGL PKLRIEEAAA RKQARIDAGK EVIVGVNKYQ TDEKTEVEVL DIDNDAVRES
QLARLTHVKA TRDDVAVKVA LAALTEAAGL RLADVAAEAQ GPEAMPHNLL ALAVTAARAR
ATLGEISDAL EAMYGRHQAT TRTVAGVYSQ EMSHNEEFAR ARAAADAFAA TEGRRPRMLV
AKMGQDGHDR GAKIIATSFA DVGFDVDLAP LFQTPGEVAR QAVDNDVHVV GVSSLAAGHK
TLLPLLIQEL KDQGRPDILV IAGGVIPAQD YQFLFNAGVA GVYGPGTVIA KAAQEILEKL
EG
//
