ID Q5QZU4_IDILO Unreviewed; 292 AA.
AC Q5QZU4;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 112.
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:AAV82267.1};
GN OrderedLocusNames=IL1427 {ECO:0000313|EMBL:AAV82267.1};
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV82267.1, ECO:0000313|Proteomes:UP000001171};
RN [1] {ECO:0000313|EMBL:AAV82267.1, ECO:0000313|Proteomes:UP000001171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC {ECO:0000313|Proteomes:UP000001171};
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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; AE017340; AAV82267.1; -; Genomic_DNA.
DR RefSeq; WP_011234673.1; NC_006512.1.
DR AlphaFoldDB; Q5QZU4; -.
DR STRING; 283942.IL1427; -.
DR KEGG; ilo:IL1427; -.
DR eggNOG; COG2513; Bacteria.
DR HOGENOM; CLU_027389_3_2_6; -.
DR OrthoDB; 9771433at2; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000001171; 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};
KW Pyruvate {ECO:0000313|EMBL:AAV82267.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001171}.
FT BINDING 46..48
FT /ligand="substrate"
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 88
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 292 AA; 31893 MW; CE5D25A90380DAB4 CRC64;
MTHMTSPGAK LRQAIADENP LQIVGTINAY TAMMAEKVGH KALYLSGAGV ANASFGLPDL
GMTSLNDVCE DIRRITAATD LPLLVDADTG WGGAFNIART VQEMTRAGAA GMHIEDQVAQ
KRCGHRPNKE IVTQEEMVDR VKAAVDARID DQFLIMARTD ALQQQGLEAA IERAQACVDA
GADAIFAEAV HTLDQYKAFT EALNVPVLAN ITEFGATPLF NKQELADVGV EIVLYPLSAF
RAMNKAALNV YNSILENGDQ KAVIDDMQTR AELYDFLNYH DFEEKLDQLF KK
//
