ID K2JFJ3_9PROT Unreviewed; 301 AA.
AC K2JFJ3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Methylisocitrate lyase {ECO:0000256|RuleBase:RU361121};
DE EC=4.1.3.30 {ECO:0000256|RuleBase:RU361121};
GN ORFNames=P24_12392 {ECO:0000313|EMBL:EKE73923.1};
OS Oceanibaculum indicum P24.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Oceanibaculaceae; Oceanibaculum.
OX NCBI_TaxID=1207063 {ECO:0000313|EMBL:EKE73923.1, ECO:0000313|Proteomes:UP000006746};
RN [1] {ECO:0000313|EMBL:EKE73923.1, ECO:0000313|Proteomes:UP000006746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P24 {ECO:0000313|EMBL:EKE73923.1,
RC ECO:0000313|Proteomes:UP000006746};
RX PubMed=23209207; DOI=10.1128/JB.01859-12;
RA Lai Q., Shao Z.;
RT "Genome Sequence of Oceanibaculum indicum Type Strain P24.";
RL J. Bacteriol. 194:6942-6942(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}.
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:EKE73923.1}.
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DR EMBL; AMRL01000015; EKE73923.1; -; Genomic_DNA.
DR RefSeq; WP_008945084.1; NZ_AMRL01000015.1.
DR AlphaFoldDB; K2JFJ3; -.
DR STRING; 1207063.P24_12392; -.
DR PATRIC; fig|1207063.3.peg.2504; -.
DR eggNOG; COG2513; Bacteria.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000006746; 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};
KW Pyruvate {ECO:0000313|EMBL:EKE73923.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006746}.
SQ SEQUENCE 301 AA; 32392 MW; 1516C82A42AC46C6 CRC64;
MPYLIADDLP TEPAGQRFRK LVERPGILGI PGSHNGMAAL QAKKAGFESL YLSGAAMTAS
MGIPDLGIIT VDEVCFFIRQ VARASGLPVL VDGDTGYGEA LNVMHMVRSF EDAGAGAVHI
EDQLLPKKCG HLNDKKLADA RDMAAKVAAA AKARRHLYVI ARTDAAASEG LDGAVARAKL
YMEAGADAIF PEALNSAEMF REFAKRMPGV PLLANMTEFG RTPFFTAKEF EEMGYRMVIW
PVSSLRVANK AQEKLYATLK QNGSTEAMAG EMQTRAELYD TIGLAKYEAL DASIVATVLP
S
//
