ID H8ILQ3_MYCIA Unreviewed; 305 AA.
AC H8ILQ3;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Methylisocitrate lyase {ECO:0000256|RuleBase:RU361121};
DE EC=4.1.3.30 {ECO:0000256|RuleBase:RU361121};
GN OrderedLocusNames=OCU_03050 {ECO:0000313|EMBL:AFC41525.1};
OS Mycobacterium intracellulare (strain ATCC 13950 / DSM 43223 / JCM 6384 /
OS NCTC 13025 / 3600).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=487521 {ECO:0000313|EMBL:AFC41525.1, ECO:0000313|Proteomes:UP000008004};
RN [1] {ECO:0000313|EMBL:AFC41525.1, ECO:0000313|Proteomes:UP000008004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13950 / DSM 43223 / JCM 6384 / NCTC 13025 / 3600
RC {ECO:0000313|Proteomes:UP000008004};
RX PubMed=22535933; DOI=10.1128/JB.00295-12;
RA Kim B.J., Choi B.S., Lim J.S., Choi I.Y., Lee J.H., Chun J., Kook Y.H.,
RA Kim B.J.;
RT "Complete genome sequence of Mycobacterium intracellulare strain ATCC
RT 13950T.";
RL J. Bacteriol. 194:2750-2750(2012).
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; CP003322; AFC41525.1; -; Genomic_DNA.
DR RefSeq; WP_009956714.1; NZ_CP076382.1.
DR AlphaFoldDB; H8ILQ3; -.
DR GeneID; 77304209; -.
DR KEGG; mia:OCU_03050; -.
DR PATRIC; fig|487521.10.peg.307; -.
DR eggNOG; COG2513; Bacteria.
DR HOGENOM; CLU_027389_3_2_11; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000008004; 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}.
SQ SEQUENCE 305 AA; 32277 MW; 907A7094A279767B CRC64;
MGGLIGGAVP ATDKRARFRA ALESGRLQRF PGAFSPLVAK LVAELGFDGV YVSGAALSAD
LGLPDIGLTT LTEVSGRGAQ IAGVSDLPTL IDADTGFGEP MSAARTVTVL EDAGLAGCHL
EDQENPKRCG HLDGKAVVPA GEMIKRLRAA VSARRDPNFI VCARTDAAGI EGVGAAIERA
KAYADAGADL IFTEALGSPT EFERFRAAVD TPLLANMTEF GKSPLLTTQQ LSDIGYNVVI
YPVTTLRLAM HAVEAGLREI AETGTQSGLT ERMQHRSRLY ELLRYADYTQ FDSDLYNFSV
QGVAP
//
