ID A0A225VKJ0_9STRA Unreviewed; 755 AA.
AC A0A225VKJ0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, 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=PHMEG_00021886 {ECO:0000313|EMBL:OWZ05933.1};
OS Phytophthora megakarya.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4795 {ECO:0000313|EMBL:OWZ05933.1, ECO:0000313|Proteomes:UP000198211};
RN [1] {ECO:0000313|Proteomes:UP000198211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=zdho120 {ECO:0000313|Proteomes:UP000198211};
RA Ali S., Shao J., Larry D.J., Kronmiller B., Shen D., Strem M.D.,
RA Melnick R.L., Guiltinan M.J., Tyler B.M., Meinhardt L.W., Bailey B.A.;
RT "Phytopthora megakarya and P. palmivora, two closely related causual agents
RT of cacao black pod achieved similar genome size and gene model numbers by
RT different mechanisms.";
RL Submitted (MAR-2017) 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:OWZ05933.1}.
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DR EMBL; NBNE01004189; OWZ05933.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A225VKJ0; -.
DR STRING; 4795.A0A225VKJ0; -.
DR EnsemblProtists; OWZ05933; OWZ05933; PHMEG_00021886.
DR OrthoDB; 304517at2759; -.
DR Proteomes; UP000198211; 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; 2.
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; 2.
DR NCBIfam; TIGR00641; acid_CoA_mut_N; 2.
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; 2.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 2.
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:UP000198211}.
FT DOMAIN 598..750
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 755 AA; 82786 MW; 973C464D4AF094C7 CRC64;
MASKELKGKD PTTHLVWHTP EGIPIKPLYT QKDLDDLELV QAPGAFPFTR GPYASMYTAK
PWTVRQYAGF STAEESNAFY RKNLAAGQQG LSVAFDLATH RGYDSDHPRV HGDVGMAGVP
IDSIADMKVL FDGIPLDKMS VSMTMNGAVL PILAMYIVTA EEQGVDQKLL SGTIQNDILK
EFMVRNTFIY PPTPSMRIIQ DIFGRRERMR MRIIQDIFGY TSEYMPKYNS ISISGYHMQE
AGADARLELA FTIADGIEYV RAAQAAGLDV DAVAPRLSFF FAIGMNFYME VAKLRAARKL
WANLMKDKFQ PKNGKSLLLR THCQTSGYSL TEQDPYNNIM RTTVEAMAAV MGGTQSLHTN
ALDEALGLPT EFSARLARNT QLVLQEETGI PRVADPWGGS YLMETLTQEL YDAALEVINE
VEELGGMAKA IESGMAKLRI EESATKKQAR VDSREETIVG VNKYVVENPD TVDVLTIDNT
TVRKKQIARI KETKANRGEE AAQASLQKLR DSAALTESTG PGKHPMNLLK LAVNAARARC
TVGEISEALE DVWGRHIPKS SVVSGAYRNE YKHNEEAEAE YNAVVKEIEA FSERFGRRPR
MLVAKMGQDG HDRGAKVIAS GYSDMGFDVD VGPLFSVIAS GYSDMGFDVD VGPLFSTPEE
SARQAVDADV HCIGVSSLAA GHNTLVPALV EALKKENAEH ILVICGGVIP PKDYQFLYDA
GVGAIFGPGT RLPISALETL RAIIKKSEEN AAKGL
//
