ID   PCMA_XANP2              Reviewed;         559 AA.
AC   A7IQE5;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Pivalyl-CoA mutase large subunit {ECO:0000303|PubMed:26134562};
DE            Short=PCM large subunit {ECO:0000303|PubMed:26134562};
DE            EC=5.4.99.- {ECO:0000269|PubMed:26134562};
DE   AltName: Full=Pivalyl-CoA mutase, substrate-binding subunit {ECO:0000303|PubMed:26134562};
GN   OrderedLocusNames=Xaut_5043 {ECO:0000312|EMBL:ABS70241.1};
OS   Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OG   Plasmid pXAUT01 {ECO:0000312|EMBL:ABS70241.1,
OG   ECO:0000312|Proteomes:UP000002417}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=78245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1158 / Py2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT   "Complete sequence of plasmid pXAUT01 of Xanthobacter autotrophicus Py2.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, BIOTECHNOLOGY, AND SUBUNIT.
RC   STRAIN=ATCC BAA-1158 / Py2;
RX   PubMed=26134562; DOI=10.1074/jbc.m115.646299;
RA   Kitanishi K., Cracan V., Banerjee R.;
RT   "Engineered and native coenzyme B12-dependent isovaleryl-CoA/pivalyl-CoA
RT   mutase.";
RL   J. Biol. Chem. 290:20466-20476(2015).
CC   -!- FUNCTION: Together with Xaut_5044, catalyzes the reversible
CC       isomerization between pivalyl-CoA and isovaleryl-CoA, using radical
CC       chemistry. Does not exhibit isobutyryl-CoA mutase (ICM) activity.
CC       {ECO:0000269|PubMed:26134562}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methylbutanoyl-CoA = 2,2-dimethylpropanoyl-CoA;
CC         Xref=Rhea:RHEA:52620, ChEBI:CHEBI:57345, ChEBI:CHEBI:136712;
CC         Evidence={ECO:0000269|PubMed:26134562};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.37 mM for isovaleryl-CoA {ECO:0000269|PubMed:26134562};
CC         Note=kcat is 14 min(-1) (measured in the presence of the small and
CC         large subunits). {ECO:0000269|PubMed:26134562};
CC   -!- SUBUNIT: Homodimer in the absence of the PCM small subunit. Weakly
CC       interacts with the PCM small subunit; an alpha(2)beta(2) stoichiometry
CC       seems to represent the active state of the enzyme.
CC       {ECO:0000269|PubMed:26134562}.
CC   -!- BIOTECHNOLOGY: This enzyme and the derivative PCM-F, a variant in which
CC       the alpha and beta subunits are fused into a single polypeptide via a
CC       short 11-amino acid linker, have potential applications in
CC       bioremediation of pivalic acid found in sludge, in stereospecific
CC       synthesis of C5 carboxylic acids and alcohols, and in the production of
CC       potential commodity and specialty chemicals.
CC       {ECO:0000305|PubMed:26134562}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA mutase large subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CP000782; ABS70241.1; -; Genomic_DNA.
DR   RefSeq; WP_011993145.1; NC_009717.1.
DR   AlphaFoldDB; A7IQE5; -.
DR   SMR; A7IQE5; -.
DR   STRING; 78245.Xaut_5043; -.
DR   EnsemblBacteria; ABS70241; ABS70241; Xaut_5043.
DR   KEGG; xau:Xaut_5043; -.
DR   eggNOG; COG1884; Bacteria.
DR   HOGENOM; CLU_009523_5_1_5; -.
DR   OrthoDB; 154460at2; -.
DR   PhylomeDB; A7IQE5; -.
DR   SABIO-RK; A7IQE5; -.
DR   Proteomes; UP000002417; Plasmid pXAUT01.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:InterPro.
DR   GO; GO:0034784; F:pivalyl-CoA mutase activity; IDA:UniProtKB.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; IDA:UniProtKB.
DR   InterPro; IPR016176; Cbl-dep_enz_cat.
DR   InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
DR   InterPro; IPR006098; MMCoA_mutase_a_cat.
DR   Pfam; PF01642; MM_CoA_mutase; 1.
DR   SUPFAM; SSF51703; SSF51703; 1.
DR   TIGRFAMs; TIGR00641; acid_CoA_mut_N; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Plasmid; Reference proteome.
FT   CHAIN           1..559
FT                   /note="Pivalyl-CoA mutase large subunit"
FT                   /id="PRO_0000434610"
SQ   SEQUENCE   559 AA;  61992 MW;  783227DC9834513E CRC64;
     MNQAAVQLPL PGFEQASGQW RSDYSRQVAG EKPVRNRSGI EVQPLYSPRD WAGERYLDDL
     GFPGQYPFTR GIYPSMHRGR TWTQRQLIGL GTPQDYNVRV RRIIDAGATA ISLLPCCSGF
     RGIDCDEVDP VLLGTCGTVV NTTDHMDAAL DGVPLGTIST AMNDPSPFTL LAFTLGVARR
     RGIDWRSITG TSNQSDYISH FIANHQFYRL SLPGSRRVLL DHIEFCRRAL PNWNPLSVVG
     QHMQQAGATP AETMGFTLSS AIQYAQDCIE RGMDVDDVLR RFTFFFDISI SFFEEIAKFR
     AGRRIWARIA RERLGAKDPA CWRFKFHGQT SGVDLTQQQP LNNIARVSVQ AMAGILSGLQ
     SMHTDAYDEA IACPSEETAR IAVATQNILR DEAQLCAVID PLGGSYYVER LTDQMEAEIE
     AVIARIDAAG GMYKAAEVGL VQTMIGESAL AFQEQLETGE RKIVGVNCYQ VEEDPTIPPA
     ERPDPEAMER HVERFKVFKR ERSQDAVARA LDALARAANS ERENVFEKVV EAAEAGVTHG
     EMVGCLRREL GFGHPLIIA