ID M7SI68_SALDU Unreviewed; 295 AA.
AC M7SI68;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 13-SEP-2023, entry version 41.
DE RecName: Full=2-methylisocitrate lyase {ECO:0000256|HAMAP-Rule:MF_01939};
DE Short=2-MIC {ECO:0000256|HAMAP-Rule:MF_01939};
DE Short=MICL {ECO:0000256|HAMAP-Rule:MF_01939};
DE EC=4.1.3.30 {ECO:0000256|HAMAP-Rule:MF_01939};
DE AltName: Full=(2R,3S)-2-methylisocitrate lyase {ECO:0000256|HAMAP-Rule:MF_01939};
GN Name=prpB {ECO:0000256|HAMAP-Rule:MF_01939};
GN ORFNames=A670_00152 {ECO:0000313|EMBL:EMR54565.1};
OS Salmonella enterica subsp. enterica serovar Dublin str. UC16.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1192688 {ECO:0000313|EMBL:EMR54565.1, ECO:0000313|Proteomes:UP000013259};
RN [1] {ECO:0000313|EMBL:EMR54565.1, ECO:0000313|Proteomes:UP000013259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC16 {ECO:0000313|EMBL:EMR54565.1,
RC ECO:0000313|Proteomes:UP000013259};
RA McClelland M., Porwollik S., Desai P., Cheng P., Wollam A., Pepin K.,
RA Bhonagiri V., Fulton L., Fulton R., Delehaunty K., Fronick C., Godfrey J.,
RA Waligorski J., Appelbaum E., Tomlinson C., Warren W., Sodergren E.,
RA Weinstock G., Wilson R.K.;
RL Submitted (FEB-2013) 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 -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the 2-methylcitrate cycle (propionate degradation route). Catalyzes
CC the thermodynamically favored C-C bond cleavage of (2R,3S)-2-
CC methylisocitrate to yield pyruvate and succinate via an alpha-carboxy-
CC carbanion intermediate. {ECO:0000256|HAMAP-Rule:MF_01939}.
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|HAMAP-Rule:MF_01939,
CC ECO:0000256|RuleBase:RU361121};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01939};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000256|HAMAP-Rule:MF_01939, ECO:0000256|RuleBase:RU361121}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000256|HAMAP-
CC Rule:MF_01939}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Methylisocitrate lyase family. {ECO:0000256|ARBA:ARBA00009282,
CC ECO:0000256|HAMAP-Rule:MF_01939, 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:EMR54565.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; APMR01000003; EMR54565.1; -; Genomic_DNA.
DR RefSeq; WP_000052227.1; NZ_KB731378.1.
DR AlphaFoldDB; M7SI68; -.
DR PATRIC; fig|1192688.3.peg.145; -.
DR HOGENOM; CLU_027389_3_2_6; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000013259; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:UniProtKB-UniRule.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR HAMAP; MF_01939; PrpB; 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|HAMAP-Rule:MF_01939, ECO:0000256|RuleBase:RU361121};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01939};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01939}.
FT BINDING 45..47
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 123..124
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 210..212
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
SQ SEQUENCE 295 AA; 31977 MW; B8BFC2A73383F052 CRC64;
MSLHSPGQAF RAALAKENPL QIVGAINANH ALLAQRAGYQ AIYLSGGGVA AGSLGLPDLG
ISTLDDVLTD IRRITDVCPL PLLVDADIGF GSSAFNVART VKSIAKAGAA ALHIEDQVGA
KRCGHRPNKA IVSKEEMVDR IRAAVDARTD PNFVIMARTD ALAVEGLEVA LDRAQAYVDA
GADMLFPEAI TELSMYRQFA DVAQVPILAN ITEFGATPLF TTDELRSANV AMALYPLSAF
RAMNRAAEKV YTVLRQEGTQ KNVIDIMQTR NELYESINYY QFEEKLDALY RNKKS
//
