ID A0A0P0SDI5_9PSEU Unreviewed; 302 AA.
AC A0A0P0SDI5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-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=AD017_16025 {ECO:0000313|EMBL:ALL82310.1};
OS Pseudonocardia sp. EC080619-01.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL82310.1, ECO:0000313|Proteomes:UP000066228};
RN [1] {ECO:0000313|EMBL:ALL82310.1, ECO:0000313|Proteomes:UP000066228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL82310.1,
RC ECO:0000313|Proteomes:UP000066228};
RX PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA Van Arnam E.B., Sit C.S.;
RT "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL J. Am. Chem. Soc. 137:14272-14274(2015).
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; CP012184; ALL82310.1; -; Genomic_DNA.
DR RefSeq; WP_060574718.1; NZ_CP012184.1.
DR AlphaFoldDB; A0A0P0SDI5; -.
DR STRING; 1096856.AD017_16025; -.
DR KEGG; pecq:AD017_16025; -.
DR PATRIC; fig|1096856.3.peg.3365; -.
DR OrthoDB; 9771433at2; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000066228; 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:ALL82310.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000066228}.
SQ SEQUENCE 302 AA; 31976 MW; 7D13BE1192BDE1CF CRC64;
MLGTTTTAHE RRVALRDALA SGRLLQFPGA FNALSAQLIA EQGFDGVYVS GAVLSAELGL
PDVGLTTATE VAGRAATIAR ATGLPTLVDA DTGWGGPANV ARTIQTFEDA GVSGCHLEDQ
IGQKRCGHLS GKELVSTDDM CTRIRAAVRG RRDEAFVLCA RTDARAVEGM DAAVARARSY
VEAGADMVFA EALTSPDEYA AFRDALDVPL LANMTEFGRT PLLDAATLEK LGVNVVIYPV
TLLRLAMGAA EAGLAEIRRT GTQAGVVDRM QTRARLYELI RYDAYGEFDA TLAGHLDEED
PA
//
