ID D8JJ60_ACISD Unreviewed; 294 AA.
AC D8JJ60;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 ECO:0000313|EMBL:ADI92683.1};
GN OrderedLocusNames=AOLE_19005 {ECO:0000313|EMBL:ADI92683.1};
OS Acinetobacter oleivorans (strain JCM 16667 / KCTC 23045 / DR1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=436717 {ECO:0000313|EMBL:ADI92683.1, ECO:0000313|Proteomes:UP000000392};
RN [1] {ECO:0000313|EMBL:ADI92683.1, ECO:0000313|Proteomes:UP000000392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16667 / KCTC 23045 / DR1
RC {ECO:0000313|Proteomes:UP000000392};
RX PubMed=20639327; DOI=10.1128/JB.00722-10;
RA Jung J., Baek J.H., Park W.;
RT "Complete genome sequence of the diesel-degrading Acinetobacter sp. strain
RT DR1.";
RL J. Bacteriol. 192:4794-4795(2010).
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 ---------------------------------------------------------------------------
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; CP002080; ADI92683.1; -; Genomic_DNA.
DR RefSeq; WP_004706036.1; NC_014259.1.
DR AlphaFoldDB; D8JJ60; -.
DR GeneID; 9384251; -.
DR KEGG; acd:AOLE_19005; -.
DR eggNOG; COG2513; Bacteria.
DR HOGENOM; CLU_027389_3_2_6; -.
DR OrthoDB; 9771433at2; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000000392; Chromosome.
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 294 AA; 31766 MW; 09CB33B47C16C076 CRC64;
MAKQSAGQLF RDAVAQEKPL QVVGTINANH ALLAKRAGYK AIYLSGGGVA AGSLGLPDLG
ISNLDDVLTD VRRITDVCDL PLLVDADTGF GASAFNIART TKALIKFGAA AMHIEDQVGA
KRCGHRPNKA IVTQEEMVDR IKAAVDARGD DSFVIMARTD ALAVDGLQAA IDRAGAYIEA
GADMLFPEAI TELDMYKQFA QKTGAPILAN ITEFGSTPLF TTEELASADV SLALYPLSAF
RAMNKAAETV YETLRKEGTQ KNVVDIMQTR KELYERINYY AFEDYLDNAF AKKK
//
