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MUTA_PIG
ID   MUTA_PIG                Reviewed;         750 AA.
AC   Q8MI68; Q8MI71;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Methylmalonyl-CoA mutase, mitochondrial;
DE            Short=MCM;
DE            EC=5.4.99.2 {ECO:0000250|UniProtKB:P22033};
DE   AltName: Full=Methylmalonyl-CoA isomerase;
DE   Flags: Precursor;
GN   Name=MMUT; Synonyms=MUT;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Kierstein S., Peters U., Krempler A., Habermann F.A., Brenig B.;
RT   "Molecular cloning and chromosomal assignment of the porcine methylmalonyl-
RT   CoA mutase gene.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible isomerization of methylmalonyl-CoA
CC       (MMCoA) (generated from branched-chain amino acid metabolism and
CC       degradation of dietary odd chain fatty acids and cholesterol) to
CC       succinyl-CoA (3-carboxypropionyl-CoA), a key intermediate of the
CC       tricarboxylic acid cycle. {ECO:0000250|UniProtKB:P22033}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-methylmalonyl-CoA = succinyl-CoA; Xref=Rhea:RHEA:22888,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:57326; EC=5.4.99.2;
CC         Evidence={ECO:0000250|UniProtKB:P22033};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22889;
CC         Evidence={ECO:0000250|UniProtKB:P22033};
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000250|UniProtKB:P22033};
CC   -!- ACTIVITY REGULATION: Inhibited by itaconyl-CoA, a metabolite that
CC       inactivates the coenzyme B12 cofactor. {ECO:0000250|UniProtKB:P22033}.
CC   -!- SUBUNIT: Homodimer. Interacts (the apoenzyme form) with MMAA; the
CC       interaction is GTP dependent. {ECO:0000250|UniProtKB:P22033}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P22033}. Mitochondrion
CC       {ECO:0000250|UniProtKB:P22033}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P22033}.
CC   -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ496801; CAD43173.1; -; mRNA.
DR   EMBL; AJ504726; CAD43288.1; -; Genomic_DNA.
DR   RefSeq; NP_999570.1; NM_214405.1.
DR   AlphaFoldDB; Q8MI68; -.
DR   SMR; Q8MI68; -.
DR   STRING; 9823.ENSSSCP00000001889; -.
DR   PaxDb; Q8MI68; -.
DR   PeptideAtlas; Q8MI68; -.
DR   PRIDE; Q8MI68; -.
DR   GeneID; 399535; -.
DR   KEGG; ssc:399535; -.
DR   CTD; 4594; -.
DR   eggNOG; ENOG502QQ7X; Eukaryota.
DR   InParanoid; Q8MI68; -.
DR   OrthoDB; 347581at2759; -.
DR   BRENDA; 5.4.99.2; 6170.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0031419; F:cobalamin binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004494; F:methylmalonyl-CoA mutase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0019678; P:propionate metabolic process, methylmalonyl pathway; IBA:GO_Central.
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   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF01642; MM_CoA_mutase; 1.
DR   SUPFAM; SSF51703; SSF51703; 1.
DR   SUPFAM; SSF52242; SSF52242; 1.
DR   TIGRFAMs; TIGR00640; acid_CoA_mut_C; 1.
DR   TIGRFAMs; TIGR00641; acid_CoA_mut_N; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS00544; METMALONYL_COA_MUTASE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cobalamin; Cobalt; Cytoplasm; Isomerase; Metal-binding;
KW   Mitochondrion; Phosphoprotein; Reference proteome; Transit peptide.
FT   TRANSIT         1..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:P22033"
FT   CHAIN           33..750
FT                   /note="Methylmalonyl-CoA mutase, mitochondrial"
FT                   /id="PRO_0000019296"
FT   DOMAIN          614..746
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT   BINDING         50
FT                   /ligand="malonyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57384"
FT                   /evidence="ECO:0000250|UniProtKB:P22033"
FT   BINDING         96..99
FT                   /ligand="malonyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57384"
FT                   /evidence="ECO:0000250|UniProtKB:P22033"
FT   BINDING         106..110
FT                   /ligand="malonyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57384"
FT                   /evidence="ECO:0000250|UniProtKB:P22033"
FT   BINDING         216..218
FT                   /ligand="malonyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57384"
FT                   /evidence="ECO:0000250|UniProtKB:P22033"
FT   BINDING         228
FT                   /ligand="malonyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57384"
FT                   /evidence="ECO:0000250|UniProtKB:P22033"
FT   BINDING         255
FT                   /ligand="malonyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57384"
FT                   /evidence="ECO:0000250|UniProtKB:P22033"
FT   BINDING         265
FT                   /ligand="malonyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57384"
FT                   /evidence="ECO:0000250|UniProtKB:P22033"
FT   BINDING         304..306
FT                   /ligand="malonyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57384"
FT                   /evidence="ECO:0000250|UniProtKB:P22033"
FT   BINDING         627
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /ligand_part="Co"
FT                   /ligand_part_id="ChEBI:CHEBI:27638"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P22033"
FT   MOD_RES         89
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P16332"
FT   MOD_RES         212
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P16332"
FT   MOD_RES         335
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P16332"
FT   MOD_RES         343
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P16332"
FT   MOD_RES         481
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P22033"
FT   MOD_RES         595
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P16332"
FT   MOD_RES         602
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P16332"
FT   CONFLICT        339
FT                   /note="R -> P (in Ref. 1; CAD43288)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   750 AA;  83337 MW;  B12E3B345698FA20 CRC64;
     MLRAKTRLFL LSPHRLKQLK KSSGSRLVWQ RLLHQQQPLH PEWAALAKKQ LKGKNPEELI
     WHTPEGISIK PLYSSRDTKD FPEELPGVKP FTRGPYPTMY TFRPWTIRQY AGFSTVEESN
     KFYKDIIKAG QQGLSVAFDL ATHRGYDSDN PRVHGDVGMA GVAIDTVEDT KILFDGIPLE
     KMSVSMTMNG AVIPVLATFI VSGEEQGVPK EKLTGTIQND ILKEFMVRNT YIFPPEPSMK
     IIADIFQYTA KHMPKFNSIS ISGYHMQEAG ADAILELAYT IADGLEYCRT GLQAGLTIDE
     FAPRLSFFWG IGMNFYMEIA KMRAGRRLWA HLIEKMFRRK NSKSLLLRAH CQTSGWSLTE
     QDPYNNIIRT TVEAMAAVFG GTQSLHTNSF DEALGLPTVK SARIARNTQI IIQEESGIPK
     VADPWGGSYM MESLTNDVYD AALKLINEIE EMGGMAKAVA EGIPKLRIEE CAARRQARID
     SGSEVIVGVN KYQLEKEESV EVLAIDNTSV RNKQIEKLKK VNPAGIKLWL ERCLTALTAC
     AASGDGNILA LAVEATRARC TVGEITDAMK KVFGEHKAND RMVSGAYRQE FGESKEISFA
     IKRVHKFMER EGRRPRLLVA KMGQDGHDRG AKVIATGFAD LGFDVDIGPL FQTPREVAQQ
     AVDADVHAVG VSTLAAGHKT LVPELIKELS TLGRPDILVM CGGVIPPQDY EFLFEVGVSN
     VFGPGTRIPK AAVQVLNDIE KCLEKKQQSM
 
 
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