ID A0A2P8HXN2_9BACI Unreviewed; 713 AA.
AC A0A2P8HXN2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=B0H94_102244 {ECO:0000313|EMBL:PSL50967.1};
OS Salsuginibacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salsuginibacillus.
OX NCBI_TaxID=517424 {ECO:0000313|EMBL:PSL50967.1, ECO:0000313|Proteomes:UP000242310};
RN [1] {ECO:0000313|EMBL:PSL50967.1, ECO:0000313|Proteomes:UP000242310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.07653 {ECO:0000313|EMBL:PSL50967.1,
RC ECO:0000313|Proteomes:UP000242310};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) 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:PSL50967.1}.
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DR EMBL; PYAV01000002; PSL50967.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8HXN2; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000242310; 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: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:UP000242310}.
FT DOMAIN 581..713
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 713 AA; 78653 MW; 091C288B527C2CB5 CRC64;
MTNPDFTQVD FKFDRVQAAE KDNSETVETP EGIHIQPAYN AEDSRHLPHI DYVSGIPPYL
RGPYASMYIT RPWTVRQYAG YSTAEESNAF YRRNLAAGQK GLSIAFDLAT HRGYDSDNPR
VEGDVGKAGV AVDSILDMKV LFDQIPLDQM SVSMTMNGAV LPVMAFYIVA AEEQGVPKEK
LTGTIQNDIL KEYMVRNTYI YPPDMSMRII ADIFSYTSTH MPKFNSISIS GYHMQEAGAT
ADLELGYTIA DGLEYVRTGL SAGIPIDQFA PRLSFFWAVG KNYFMEVAKM RAARLIWARL
LEDYGAENPK SLTLRTHSQT SGWSLTEQDP YNNVVRTQIE AMAAAMGHTQ SLHTNALDEA
IALPTDFSAK IARNTQLHLQ EETGMTAVVD PWGGSHYVEV LTAELAEKAW AHLEEVDELG
GMAKAIETGL PKMRIEEAAA RRQAQIDAGK ETIVGVNKHR LDEEDPLDVR NIDNTEVRRA
QLERLEQLRN ERDEQGAQAA LTALSEAAAS HDINLLEKAV DAARARATLG EISDAVEKTS
GRHQAVIRSI SGVYSAEYGE DEQMELVRRR TDAFEEEEGR RPRIMIAKMG QDGHDRGAKV
VATAYADMGF DVDIGPLFQT PEEAALQAVE NDVHILGISS LAAGHKTLLP RVVEELRRLG
RDDIVVIIGG IIPPHDYEEL TEMGAAAIFG PGTVLPAAAG EVLDAVWAQV EQD
//
