ID   A0A158PH47_ANGCS        Unreviewed;       705 AA.
AC   A0A158PH47;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-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=ACOC_LOCUS5989 {ECO:0000313|EMBL:VDM57574.1};
OS   Angiostrongylus costaricensis (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC   Angiostrongylus.
OX   NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000598801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ACOC_0000598801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDM57574.1, ECO:0000313|Proteomes:UP000267027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Costa Rica {ECO:0000313|EMBL:VDM57574.1,
RC   ECO:0000313|Proteomes:UP000267027};
RG   Pathogen Informatics;
RL   Submitted (NOV-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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; UYYA01003910; VDM57574.1; -; Genomic_DNA.
DR   STRING; 334426.A0A158PH47; -.
DR   WBParaSite; ACOC_0000598801-mRNA-1; ACOC_0000598801-mRNA-1; ACOC_0000598801.
DR   OMA; IQEETHI; -.
DR   Proteomes; UP000050601; Unplaced.
DR   Proteomes; UP000267027; 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; 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:UP000267027}.
FT   DOMAIN          569..701
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   705 AA;  77688 MW;  5CBC8E04AE3AB8D8 CRC64;
     MAKKAMKGKD PNSLIWDTPE GIAIKPLYLK EDRKCDEYRE SELPGKYPFS RGPYPTMYTQ
     RPWTIRQYAG FSTVEESNAF YKENIKAGQQ GLSVAFDLAT HRGYDSDNPR VYGDVGMAGV
     AVDSVEDMKQ LFDGIPLDKM SVSMTMNGAV IPVLAMYIVA AEESGVDRKL LTGTIQNDIL
     KEFMVRNTYI YPPDPSMRII GDIFAYTSKE MPKWNSISIS GYHMQEAGAD AVLEMAFTIA
     DGIQYCQTGL DAGLTIDQFA PRLSFFWGIG MNFYMEIAKM RAARRLWANL LTEIFQPKNS
     KSLMLRTHSQ TSGWSLTEQD PYNNIIRTTI EAMASVFGGT QSLHTNSFDE ALGLPTKFSA
     RIARNTQIII QEESGICKVA DPWGGSYMME SLTDELYNKA RKVFDEITEL GGMAKAVASG
     MTKLRIEEAA AKKQARIDAA KDVIVGVNKY RLEQVVDVLH VDNQKVREKQ IAKLEHIRKT
     RDPQRAKAAL EAITKGAAGK ENLLELAVEA SRARCSVGEI SDAMEKVFTR YAAVNRMVSG
     AYKSEFGETS EIDQVMERVK AFATKEGRQP RIMIAKMGQD GHDRGAKVVA TGFADLGFDV
     DVGPLFQTPA EAAQQAVDAD VHAIGASSLA AGHLTLIPEL IQELGKLGRE DIIVIAGGVI
     PPQDYDALYK AGVSLIFGPG TRLPTCANQV LDKLEQGQEK QSAKS
//