ID A0A2Z5EKJ6_9SPHN Unreviewed; 306 AA.
AC A0A2Z5EKJ6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Methylisocitrate lyase {ECO:0000256|RuleBase:RU361121};
DE EC=4.1.3.30 {ECO:0000256|RuleBase:RU361121};
GN Name=prpB {ECO:0000313|EMBL:AXB80215.1};
GN ORFNames=TQ38_026870 {ECO:0000313|EMBL:AXB80215.1};
OS Novosphingobium sp. P6W.
OG Plasmid pp6w1 {ECO:0000313|Proteomes:UP000032296}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1609758 {ECO:0000313|EMBL:AXB80215.1, ECO:0000313|Proteomes:UP000032296};
RN [1] {ECO:0000313|EMBL:AXB80215.1, ECO:0000313|Proteomes:UP000032296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6W {ECO:0000313|EMBL:AXB80215.1,
RC ECO:0000313|Proteomes:UP000032296};
RC PLASMID=Plasmid pp6w1 {ECO:0000313|Proteomes:UP000032296};
RA Nikolaichik Y.A., Safronova V.I., Belimov A., Gogolev Y.V., Gogoleva N.E.;
RT "Complete genome sequence of Novosphingobium sp. P6W.";
RL Submitted (JUN-2018) 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; CP030354; AXB80215.1; -; Genomic_DNA.
DR RefSeq; WP_043975915.1; NZ_CP030354.1.
DR AlphaFoldDB; A0A2Z5EKJ6; -.
DR STRING; 1609758.TQ38_15640; -.
DR KEGG; nov:TQ38_026870; -.
DR OrthoDB; 9771433at2; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000032296; Plasmid pp6w1.
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:AXB80215.1};
KW Plasmid {ECO:0000313|EMBL:AXB80215.1}.
SQ SEQUENCE 306 AA; 32505 MW; 263CDD0BFC288B79 CRC64;
MPYLLADDLP TESAGKRFRA ALSRPGIYRL PGAHNGQAAI QARNAGFDGL YLSGAAMTAS
MGLPDLGIIT VDEVAFFIRQ IVRSSGLPLL VDGDTGYGEA LNVMHMVRSF EDAGAGAVHL
EDQILPKKCG HLNGKALVSP TDMAAKVAAA KKASRDIVIV ARTDAAGVEG FDGAVERAKL
YVDAGADAIF PEALNTREMF EKFAAALPDV PLLANMTEFG KTPFYTAAEF EAMGYKMVIW
PVSSLRVANK AQAKLYAAIA KDGGTHAMVD AMQTRAELYD TIGLHAYEEL DASIVKTIVP
EAIPQG
//
