ID   A0A101X8N2_9CREN        Unreviewed;       316 AA.
AC   A0A101X8N2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   13-SEP-2023, entry version 25.
DE   RecName: Full=Methylisocitrate lyase {ECO:0000256|RuleBase:RU361121};
DE            EC=4.1.3.30 {ECO:0000256|RuleBase:RU361121};
GN   ORFNames=AT715_00530 {ECO:0000313|EMBL:KUO86876.1};
OS   Thermoproteus sp. JCHS_4.
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Thermoproteus.
OX   NCBI_TaxID=1714258 {ECO:0000313|EMBL:KUO86876.1, ECO:0000313|Proteomes:UP000054781};
RN   [1] {ECO:0000313|EMBL:KUO86876.1, ECO:0000313|Proteomes:UP000054781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B.,
RA   Inskeep W.P.;
RT   "The distribution, diversity and function of predominant Thermoproteales in
RT   high-temperature environments of Yellowstone National Park.";
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}.
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:KUO86876.1}.
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DR   EMBL; LOBZ01000031; KUO86876.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101X8N2; -.
DR   STRING; 1714258.AT715_00530; -.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000054781; 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:KUO86876.1}.
SQ   SEQUENCE   316 AA;  34803 MW;  CA1A3A976A1A5A37 CRC64;
     MKAPILRKDR KDVVAELRAE LKKPGIVVVP GVYDVITALL AQSMGFKAGY VSGAAVTASL
     GLPDLGIVTM DEMVRVVRYI ASSVDMPLIV DIDTGYGEAL NVVRAVVEFE RAGAAGVQIE
     DQVLPKKCGH LSGKALVSPD EMAKKIKAAV EARRNPDFVI VARTDARGVA GFDDAVERAR
     LYLEVGADVI FPEALESEQE FAEFARRVKA PLLANMTEFG KSPLIPAKRL EEYGYKFVIF
     PVTLLRVALG AVRDALRTIA ELGTQEPLVP RMLTRKELYE LIGYYDYEDF DKKIAEEVDR
     RLAVKLRPDK VHGQDN
//