ID A0A1I3CH44_9MICO Unreviewed; 305 AA.
AC A0A1I3CH44;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:TFB88822.1};
GN ORFNames=E3O11_01955 {ECO:0000313|EMBL:TFB88822.1};
OS Cryobacterium levicorallinum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=995038 {ECO:0000313|EMBL:TFB88822.1, ECO:0000313|Proteomes:UP000297963};
RN [1] {ECO:0000313|EMBL:TFB88822.1, ECO:0000313|Proteomes:UP000297963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hh34 {ECO:0000313|EMBL:TFB88822.1,
RC ECO:0000313|Proteomes:UP000297963};
RA Liu Q., Xin Y.-H.;
RT "Genomics of glacier-inhabiting Cryobacterium strains.";
RL Submitted (MAR-2019) 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:TFB88822.1}.
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DR EMBL; SOFE01000003; TFB88822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3CH44; -.
DR STRING; 995038.SAMN05216274_11344; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000297963; 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:TFB88822.1}.
SQ SEQUENCE 305 AA; 32941 MW; 60299EC8F953CC6F CRC64;
MLYARRDAAD KRIALRQGLK SGKILRFPGA FNPLSAKLIQ QKGFEGVYIS GAVLSADLGL
PDIGLTTLTE VAGRSQQIAR MTDLPAIVDA DTGFGEPMNV ARTIQTLEDA GLAGMHIEDQ
INPKRCGHLD GKQVVDADTA IKRIRAAVDA RRDANFLVMA RTDIRAVDGL DAAVTRAKQL
QDAGADAIFP EAMGSLAEFE TIRAAVSVPI LANMTEFGKG ELYTVQQLEN VGMNLVIFPV
SLLRLAMGSA ARGLDAIEQT GSLTTMLPEM QHRADLYELL DYASYSQFDS GIFDFTLNPH
ISSKV
//
