ID   A0A0N5C2E2_STREA        Unreviewed;       736 AA.
AC   A0A0N5C2E2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, 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};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001215200.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0001215200.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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   AlphaFoldDB; A0A0N5C2E2; -.
DR   STRING; 174720.A0A0N5C2E2; -.
DR   WBParaSite; SPAL_0001215200.1; SPAL_0001215200.1; SPAL_0001215200.
DR   Proteomes; UP000046392; Unplaced.
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}.
FT   DOMAIN          604..736
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   736 AA;  81241 MW;  4B05DD37059E639F CRC64;
     MLRIKKTASL STNILKFTRT CASLPLYPKW AEMAKKQLKG KDPESLIWHT TEGIDIKPLY
     TIKDREKDFN SGNVELPGQF PYTRGPYPTM YTQRPWTIRQ YAGFSTVEES NKFYKENIAA
     GQQGVSVAFD LPTHRGYDSD NPRVSGDVGM AGVAVDSVED MKALFDGIPL DKISVSMTMN
     GAVIPVLAMY VVAGEEQGVD QALLAGTIQN DILKEFMVRN TYIYPPEPSM RIIGDIFAYT
     AKHMPKFNSI SISGYHIQEA GADAALEMAF TIADGLQYCQ TGLDAGLTID EFAPRLSFFW
     GISMNFYMEI AKMRAARRLW ANLVKERFNP KNPRSNMLRT HCQTSGWSLT AQDPYNNIIR
     TTVEAMASIF GGTQSLHTNA FDEAICLPTK QSARIARNTQ IILQEESGIC KVADPWGGSY
     MMESLTDELY AKSYEIIKEI DEMGGMAKAV TSGMPKLKIE EAAAKKQAKI DIGEQVIVGV
     NKYKLEQETP IEILKVDNER VRGSQCAKLK RIRETRDPAR AKAAIDRIID CCKNGGNLME
     AAVEAARARV TVGEMSDAME SVFSRYAAVN RMVSGAYITS FGESREIETV LHRVTKFAER
     EGRQPRLMVA KLGQDGHDRG AKIVATGFAD LGFDVDIGPL FQTPQEAAQQ AVDADVHVIG
     ASSLAAGHLT LVPELIDELK KLGREDIMVI AGGVIPPQDY EALYAAGVSC VFGPGTRLPD
     CANEILDKLE LKFKKN
//