ID A0A0U3FNL2_9MICC Unreviewed; 309 AA.
AC A0A0U3FNL2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Methylisocitrate lyase {ECO:0000256|RuleBase:RU361121};
DE EC=4.1.3.30 {ECO:0000256|RuleBase:RU361121};
GN ORFNames=MB46_04370 {ECO:0000313|EMBL:ALV44857.1};
OS Arthrobacter alpinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=656366 {ECO:0000313|EMBL:ALV44857.1, ECO:0000313|Proteomes:UP000055883};
RN [1] {ECO:0000313|EMBL:ALV44857.1, ECO:0000313|Proteomes:UP000055883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3 {ECO:0000313|EMBL:ALV44857.1,
RC ECO:0000313|Proteomes:UP000055883};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-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}.
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DR EMBL; CP013745; ALV44857.1; -; Genomic_DNA.
DR RefSeq; WP_044571919.1; NZ_CP013745.1.
DR AlphaFoldDB; A0A0U3FNL2; -.
DR STRING; 656366.AS189_14610; -.
DR KEGG; arw:MB46_04370; -.
DR eggNOG; COG2513; Bacteria.
DR OrthoDB; 9771433at2; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000055883; Chromosome.
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:ALV44857.1}.
SQ SEQUENCE 309 AA; 33409 MW; 2D837B29168CFF68 CRC64;
MLYSKKTPEQ KRRDLRAMLV PGAAVQFPGA FNPLSARLIE EKKFDGVYIS GAVLANDLGL
PDIGMTTLTE VAARGGQIAR MTDLPCLIDA DTGFGEPMNV ARTIQELENA GLAGCHIEDQ
FNPKRCGHLD GKNMVDLDTA VKRIAAATDA RRDENFLIMA RTDIRAVEGL DTAIDRAKAL
VDAGADAIFP EAMKSVAEFE AVCNAVNVPV LANMTEFGKS ELFNRDDLAS AGVAMIIYPV
TLLRSAMGAA ERALDAISAE GTQESAVPDM LTRARLYDLV DYEAYNQFDT GIFNFQVPGL
DIERNSANL
//
