PRPB_CUPNE
ID PRPB_CUPNE Reviewed; 302 AA.
AC Q937P0;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=2-methylisocitrate lyase {ECO:0000303|PubMed:11495997};
DE Short=2-MIC {ECO:0000255|HAMAP-Rule:MF_01939};
DE Short=MICL {ECO:0000255|HAMAP-Rule:MF_01939};
DE EC=4.1.3.30 {ECO:0000269|PubMed:11495997};
DE AltName: Full=(2R,3S)-2-methylisocitrate lyase {ECO:0000255|HAMAP-Rule:MF_01939};
GN Name=prpB {ECO:0000303|PubMed:11495997};
OS Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=106590 {ECO:0000312|EMBL:AAL03988.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP PHENOTYPE, AND INDUCTION.
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: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the 2-methylcitrate cycle I (propionate degradation route).
CC Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-
CC methylisocitrate to yield pyruvate and succinate via an alpha-carboxy-
CC carbanion intermediate. {ECO:0000255|HAMAP-Rule:MF_01939,
CC ECO:0000269|PubMed:11495997}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate +
CC succinate; Xref=Rhea:RHEA:16809, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57429; EC=4.1.3.30;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01939,
CC ECO:0000269|PubMed:11495997};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01939};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000305|PubMed:11495997}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_01939}.
CC -!- INDUCTION: By propionate. {ECO:0000269|PubMed:11495997}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show an accumulation of
CC 2-methylisocitric acid. {ECO:0000269|PubMed:11495997}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Methylisocitrate lyase family. {ECO:0000305}.
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DR EMBL; AF325554; AAL03988.1; -; Genomic_DNA.
DR AlphaFoldDB; Q937P0; -.
DR SMR; Q937P0; -.
DR UniPathway; UPA00946; -.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IDA:UniProtKB.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IMP:UniProtKB.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR HAMAP; MF_01939; PrpB; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR InterPro; IPR012695; PrpB.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR SUPFAM; SSF51621; SSF51621; 1.
DR TIGRFAMs; TIGR02317; prpB; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..302
FT /note="2-methylisocitrate lyase"
FT /id="PRO_0000432931"
FT BINDING 51..53
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 129..130
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 216..218
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
SQ SEQUENCE 302 AA; 32314 MW; 1115E7BCEE2FAFA8 CRC64;
MTYSASDLAR SAGARFRQAL ADEHPLQVVG TINANHALLA KRAGYRAIYL SGGGVAAGSL
GLPDLGISNL DDVLTDIRRI TDVCDTPLLV DVDTGFGASA FNVARTTKSL IKFGAAAMHI
EDQVGAKRCG HRPNKEIVTQ GEMVDRIRAA VDARTDENFV IMARTDALAV EGLDKAIERA
VACAEAGADA IFPEAMTDLA MYRKFVDAVK VPVLANITEF GATPLFTTEE LDGAGVSMVL
LPLSAFRAMN KAAENVYAAI RQDGTQKNVV DTMQTRAELY ESIGYHDFEQ KLDALFAQGK
GK
