ID A0A0M2LY38_9MICO Unreviewed; 303 AA.
AC A0A0M2LY38;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Methylisocitrate lyase {ECO:0000256|RuleBase:RU361121};
DE EC=4.1.3.30 {ECO:0000256|RuleBase:RU361121};
GN ORFNames=XM48_07780 {ECO:0000313|EMBL:KKI20407.1};
OS Leucobacter sp. Ag1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1642040 {ECO:0000313|EMBL:KKI20407.1, ECO:0000313|Proteomes:UP000033836};
RN [1] {ECO:0000313|EMBL:KKI20407.1, ECO:0000313|Proteomes:UP000033836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI20407.1,
RC ECO:0000313|Proteomes:UP000033836};
RA Pei D., Kukutla P., Yu W., Xu J.;
RT "Draft Genome Sequences of Leucobacter sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) 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 -!- 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|RuleBase:RU361121};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000256|RuleBase:RU361121}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Methylisocitrate lyase family. {ECO:0000256|ARBA:ARBA00009282,
CC ECO:0000256|RuleBase:RU361121}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKI20407.1}.
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DR EMBL; LAYO01000092; KKI20407.1; -; Genomic_DNA.
DR RefSeq; WP_046455241.1; NZ_LAYO01000092.1.
DR AlphaFoldDB; A0A0M2LY38; -.
DR STRING; 1642040.XM48_07780; -.
DR PATRIC; fig|1642040.3.peg.542; -.
DR OrthoDB; 9771433at2; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000033836; Unassembled WGS sequence.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:InterPro.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 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|RuleBase:RU361121, ECO:0000313|EMBL:KKI20407.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033836}.
SQ SEQUENCE 303 AA; 33039 MW; C44EB10DA233EF59 CRC64;
MLYSKTTAEQ KRLALRERLA SGELLRFPGA FNPLSARLIE RKGFDGVYIS GAVLAADLGL
PDIGLTTLSE VAGRGEQIAR MTELPAIIDA DTGFGEPMNV ARTIQSLENA GIAGCHIEDQ
INPKRCGHLD GKAVVDVDTA AKRIRAAVDA RRDPNFLIMA RTDIRATADG PMGLDIAVDR
AKALVDAGAD AIFPEAMRTL EEFETMRGAV DVPLLANMTE FGKSELFSAQ QLADIGMNIV
IWPVSMLRIA MGATGRALDA LNDEGHLRGR LDEMQHRADL YDLVDYEAYN RFDSGVFNFE
VER
//
