ID   PRPF_CUPNE              Reviewed;         396 AA.
AC   Q937N7;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=2-methyl-aconitate isomerase {ECO:0000303|PubMed:11495997};
DE            EC=5.3.3.- {ECO:0000269|PubMed:11495997};
DE   AltName: Full=Cis-trans isomerase {ECO:0000303|PubMed:11495997};
OS   Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=106590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=HF39;
RX   PubMed=11495997; DOI=10.1099/00221287-147-8-2203;
RA   Bramer C.O., Steinbuchel A.;
RT   "The methylcitric acid pathway in Ralstonia eutropha: new genes identified
RT   involved in propionate metabolism.";
RL   Microbiology 147:2203-2214(2001).
CC   -!- FUNCTION: Catalyzes the isomerization of 2-methyl-trans-aconitate to
CC       yield 2-methyl-cis-aconitate through a base-catalyzed proton
CC       abstraction coupled with a rotation about C2-C3 bond of 2-methyl-
CC       aconitate. {ECO:0000269|PubMed:11495997}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-methyl-trans-aconitate = 2-methyl-cis-aconitate;
CC         Xref=Rhea:RHEA:37751, ChEBI:CHEBI:57872, ChEBI:CHEBI:58915;
CC         Evidence={ECO:0000269|PubMed:11495997};
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000305|PubMed:11495997}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8EJW4}.
CC   -!- MISCELLANEOUS: Could be involved in the catabolism of short chain fatty
CC       acids (SCFA) via the 2-methylcitrate cycle II (propionate degradation
CC       route), however it does not have a 2-methylcitrate dehydratase able to
CC       produce 2-methyl-trans-aconitate. {ECO:0000305|PubMed:11495997}.
CC   -!- SIMILARITY: Belongs to the PrpF family. {ECO:0000305}.
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DR   EMBL; AF325554; AAL03991.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q937N7; -.
DR   SMR; Q937N7; -.
DR   UniPathway; UPA00946; -.
DR   GO; GO:0016863; F:intramolecular oxidoreductase activity, transposing C=C bonds; IDA:UniProtKB.
DR   GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IDA:UniProtKB.
DR   InterPro; IPR012709; PrpF.
DR   InterPro; IPR007400; PrpF_protein.
DR   PANTHER; PTHR43709; PTHR43709; 1.
DR   Pfam; PF04303; PrpF; 1.
DR   TIGRFAMs; TIGR02334; prpF; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Oxidation.
FT   CHAIN           1..396
FT                   /note="2-methyl-aconitate isomerase"
FT                   /id="PRO_0000432937"
FT   ACT_SITE        104
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8EJW4"
FT   ACT_SITE        318
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8EJW4"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8EJW4"
FT   BINDING         66..70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8EJW4"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8EJW4"
FT   BINDING         278
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8EJW4"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8EJW4"
FT   BINDING         314
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8EJW4"
FT   BINDING         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8EJW4"
FT   MOD_RES         104
FT                   /note="Cysteine sulfinic acid (-SO2H)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8EJW4"
SQ   SEQUENCE   396 AA;  41514 MW;  278188D8E0B44F45 CRC64;
     MTHVPQIKIP ATYIRGGTSK GVFFRLQDLP ETAQVPGPAR DALLMRVIGS PDPYGKQIDG
     MGAATSSTSK TVILSKSTRP DHDVDYLFGQ VSIDQPFVDW SGNCGNLSAA VGPFAISAGL
     VDASRIPHNG VAVVRIWQAN IGKTIIGHVP VTNGEVQETG DFELDGVTFP AAEVQLEFMD
     PAAEEEGAGG AMFPTGNVVD DLEVPAVGTL KATMINAGIP TIFVNAESIG YTGTELQDAI
     NSDTRALAMF EDHPCYGALR MGLIKNVDEA AKRQHTPKVA FVRQAGDYVA SSGKKVAAAD
     VDLLVRALSM GKLHHAMMGT AAVAIGTAAA IPGTLVNLAA GGGERNAVRF GHPSGTLRVG
     AEAQQVDGEW AVKKAIMSRS ARVLMEGWVR VPGDAF