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
//