ID E0I603_9BACL Unreviewed; 295 AA.
AC E0I603;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=PaecuDRAFT_1075 {ECO:0000313|EMBL:EFM12395.1};
OS Paenibacillus curdlanolyticus YK9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM12395.1, ECO:0000313|Proteomes:UP000005387};
RN [1] {ECO:0000313|EMBL:EFM12395.1, ECO:0000313|Proteomes:UP000005387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YK9 {ECO:0000313|EMBL:EFM12395.1,
RC ECO:0000313|Proteomes:UP000005387};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL Submitted (JUL-2010) 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}.
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DR EMBL; AEDD01000002; EFM12395.1; -; Genomic_DNA.
DR RefSeq; WP_006037090.1; NZ_AEDD01000002.1.
DR AlphaFoldDB; E0I603; -.
DR STRING; 717606.PaecuDRAFT_1075; -.
DR eggNOG; COG2513; Bacteria.
DR OrthoDB; 8629576at2; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000005387; 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|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01939};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01939}; Reference proteome {ECO:0000313|Proteomes:UP000005387}.
FT BINDING 44..46
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 121..122
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 208..210
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01939"
SQ SEQUENCE 295 AA; 31908 MW; BE4F11E3EA4F833F CRC64;
MRQSAGQRLR SAVEAERPLQ VAGAINAYAA MMAEQVGFRA LYVSGAGVAN ASFGLPDLGI
TSLNDCVEDV RRLSSVTELP ILVDADTGFG SAFQIARTVQ QMERAGAAGI HIEDQVAAKR
CGHRPNKAIV SQAEMTDRIR AAADARADSQ FVIMARTDAL AVEGIDRAIE RARACVEAGA
DMIFPEAVTR LEDYKAFAEA VQVPVLANIT EFGLTPLFTT EQLASAGVGL ALYPLSAFRA
MSAAALLVYK AIREEGTQQS VIDRMQTRSE LYAFLHYLDY EQRLDRLFGI EKGVD
//
