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Database: UniProt
Entry: A0A1B1ZXF0_9PSEU
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ID   A0A1B1ZXF0_9PSEU        Unreviewed;       739 AA.
AC   A0A1B1ZXF0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE            EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN   ORFNames=AFB00_26555 {ECO:0000313|EMBL:ANY10431.1};
OS   Pseudonocardia sp. HH130630-07.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1690815 {ECO:0000313|EMBL:ANY10431.1, ECO:0000313|Proteomes:UP000092926};
RN   [1] {ECO:0000313|EMBL:ANY10431.1, ECO:0000313|Proteomes:UP000092926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HH130630-07 {ECO:0000313|EMBL:ANY10431.1,
RC   ECO:0000313|Proteomes:UP000092926};
RA   Oliw E.H.;
RL   Submitted (JAN-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   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000256|ARBA:ARBA00011870}.
CC   -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC       {ECO:0000256|ARBA:ARBA00008465}.
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DR   EMBL; CP013854; ANY10431.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B1ZXF0; -.
DR   STRING; 1690815.AFB00_26555; -.
DR   KEGG; phh:AFB00_26555; -.
DR   OrthoDB; 9762378at2; -.
DR   Proteomes; UP000092926; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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.
PE   3: Inferred from homology;
KW   Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW   Cobalt {ECO:0000256|ARBA:ARBA00022628};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092926}.
FT   DOMAIN          593..725
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   739 AA;  79559 MW;  773B6AF907E0B6E0 CRC64;
     MEVTGIPDFT EVPLRSATTP STGWTGSAPT WDAPEGIGVR PLYTARDLDG LDFLGTYPGI
     TPYLRGPYPT MYTNQPWTVR QYAGFSTAAE SNAFYRRNLA AGQKGLSIAF DLATHRGYDS
     DHPRVGGDVG MAGVAIDSIL DMRQLFDGIP LDRMSVSMTM NGAVLPVLAL YIVAAEEQGV
     APKALTGTIQ NDILKEFMVR NTYIYPPQPS MQIISDIFGY TSANMPKFNS ISISGYHIQE
     AGATNDLELA YTLADGVEYL RAGVDAGLDV DTFAPRLSFF WAIGMNFFME VAKMRAARLL
     WSKLVNRFEP QNAKSLSLRT HSQTSGWSLT AQDVYNNVVR TCVEAMAATQ GHTQSLHTNA
     LDEALALPTD FSARIARNTQ LLLQQESGTT DVVDPWGGSY YVERLTYDLA RRAWAHIEEV
     ESAGGMAAAI DAGIPKMRVE EAAARTQARI DSGRQPVIGV NKYALTADEQ IDVLKVDNAN
     VRREQLEKLR TLRAERDDRA LDDSLRRLTG VAEKIAEGGR RDDADNLLGL AVDAARNKAT
     VGEISDALEK VFGRHAGQIR IISGVYSAEA GQNPAIDRAR ELVSDFAGHE GRQPRILVAK
     MGQDGHDRGQ KVIATAFADI GFDVDVGPLF QTPAEVAKQA VESDVHVIGA SSLAAGHLTL
     VPELRSELAE LGREDIMVVV GGVIPPADVP ELLEMGAAAV FPPGTVIAEA AVDLLGKLAV
     ALGHDEGDAA AAPGSVFAD
//
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