ID A0A1L6I8J6_9BURK Unreviewed; 307 AA.
AC A0A1L6I8J6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=2-methylisocitrate lyase {ECO:0000256|HAMAP-Rule:MF_01939};
DE Short=2-MIC {ECO:0000256|HAMAP-Rule:MF_01939};
DE Short=MICL {ECO:0000256|HAMAP-Rule:MF_01939};
DE EC=4.1.3.30 {ECO:0000256|HAMAP-Rule:MF_01939};
DE AltName: Full=(2R,3S)-2-methylisocitrate lyase {ECO:0000256|HAMAP-Rule:MF_01939};
GN Name=prpB {ECO:0000256|HAMAP-Rule:MF_01939};
GN ORFNames=BTO02_30055 {ECO:0000313|EMBL:APR39500.1};
OS Paraburkholderia sp. SOS3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1926494 {ECO:0000313|EMBL:APR39500.1, ECO:0000313|Proteomes:UP000184708};
RN [1] {ECO:0000313|EMBL:APR39500.1, ECO:0000313|Proteomes:UP000184708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SOS3 {ECO:0000313|EMBL:APR39500.1,
RC ECO:0000313|Proteomes:UP000184708};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the thermodynamically favored C-C bond cleavage of
CC (2R,3S)-2-methylisocitrate to yield pyruvate and succinate.
CC {ECO:0000256|RuleBase:RU361121}.
CC -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the 2-methylcitrate cycle (propionate degradation route). Catalyzes
CC 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:0000256|HAMAP-Rule:MF_01939}.
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:0000256|HAMAP-Rule:MF_01939,
CC ECO:0000256|RuleBase:RU361121};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01939};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000256|HAMAP-Rule:MF_01939, ECO:0000256|RuleBase:RU361121}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000256|HAMAP-
CC Rule:MF_01939}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Methylisocitrate lyase family. {ECO:0000256|ARBA:ARBA00009282,
CC ECO:0000256|HAMAP-Rule:MF_01939, ECO:0000256|RuleBase:RU361121}.
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DR EMBL; CP018812; APR39500.1; -; Genomic_DNA.
DR RefSeq; WP_075160670.1; NZ_CP018812.1.
DR AlphaFoldDB; A0A1L6I8J6; -.
DR STRING; 1926494.BTO02_30055; -.
DR KEGG; para:BTO02_30055; -.
DR OrthoDB; 9771433at2; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000184708; Chromosome 2.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:UniProtKB-UniRule.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 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 NCBIfam; TIGR02317; prpB; 1.
DR PANTHER; PTHR42905:SF5; CARBOXYVINYL-CARBOXYPHOSPHONATE PHOSPHORYLMUTASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01939, ECO:0000256|RuleBase:RU361121};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01939};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01939}.
FT BINDING 58..60
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 136..137
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 223..225
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
SQ SEQUENCE 307 AA; 32634 MW; 6A0D3CEEF3332FCC CRC64;
MTPTTEPSTN TAAHAQTSAG ARFRAAVAAE KPLQVVGAIN ANHALLAQHA GFKAIYVSGG
GVAAGSLGLP DLGISTLDDV LTDVRRITDV CDLPLLVDVD TGFGPSAFNI ARTVKALTKA
GAGAMHIEDQ VGAKRCGHRP GKAIVSQDEM VDRIKAAVDA RTDPAFVIMA RTDALAVDGL
QAAIDRAAAC VEAGADMIFP EAMTELDMYR QFVKAVKVPV LANITEFGAT PLFTVDELRG
ADVSLVLYPL SAFRAMNRAA ENVYRTIRRD GTQQAVVDTM QTRAELYESI GYYAYEQKLD
ELFSGSR
//
