PCMB_XANP2
ID PCMB_XANP2 Reviewed; 148 AA.
AC A7IQE6;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Pivalyl-CoA mutase small subunit {ECO:0000303|PubMed:26134562};
DE Short=PCM small subunit {ECO:0000303|PubMed:26134562};
DE EC=5.4.99.- {ECO:0000269|PubMed:26134562};
DE AltName: Full=Pivalyl-CoA mutase, AdoCbl-binding subunit {ECO:0000303|PubMed:26134562};
GN OrderedLocusNames=Xaut_5044 {ECO:0000312|EMBL:ABS70242.1};
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OG Plasmid pXAUT01 {ECO:0000312|EMBL:ABS70242.1,
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, COFACTOR, 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_5043, 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 -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000269|PubMed:26134562};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 14 min(-1) (measured in the presence of the small and
CC large subunits). {ECO:0000269|PubMed:26134562};
CC -!- SUBUNIT: Monomer in the absence of the PCM large subunit. Weakly
CC interacts with the PCM large 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 small subunit family.
CC {ECO:0000305}.
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DR EMBL; CP000782; ABS70242.1; -; Genomic_DNA.
DR RefSeq; WP_011993146.1; NC_009717.1.
DR AlphaFoldDB; A7IQE6; -.
DR SMR; A7IQE6; -.
DR STRING; 78245.Xaut_5044; -.
DR EnsemblBacteria; ABS70242; ABS70242; Xaut_5044.
DR KEGG; xau:Xaut_5044; -.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_128233_0_0_5; -.
DR OMA; VECVTAL; -.
DR OrthoDB; 1335734at2; -.
DR PhylomeDB; A7IQE6; -.
DR SABIO-RK; A7IQE6; -.
DR Proteomes; UP000002417; Plasmid pXAUT01.
DR GO; GO:0031419; F:cobalamin binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034784; F:pivalyl-CoA mutase activity; IDA:UniProtKB.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IDA:UniProtKB.
DR InterPro; IPR006159; Acid_CoA_mut_C.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR Pfam; PF02310; B12-binding; 1.
DR SUPFAM; SSF52242; SSF52242; 1.
DR TIGRFAMs; TIGR00640; acid_CoA_mut_C; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
PE 1: Evidence at protein level;
KW Cobalamin; Cobalt; Isomerase; Metal-binding; Plasmid; Reference proteome.
FT CHAIN 1..148
FT /note="Pivalyl-CoA mutase small subunit"
FT /id="PRO_0000434611"
FT DOMAIN 8..138
FT /note="B12-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT BINDING 21
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:Q1LRY0"
SQ SEQUENCE 148 AA; 15549 MW; A59701B2C8BA0D1E CRC64;
MIHAGTRPLR VLVTKIGLDG HDRGSRIVAA YLRDAGMEVI YTPPWQTIPG VVKLATEEDV
DVIGISSLAT DHLIVPKMME ALRAAGLGHV GVVVGGIVPE AEQSALAAAG VSRVFGPGAA
REEIVECVTA LGQKSRAERV DDYSEANP
