ID A0A0Q2L993_XYLFS Unreviewed; 298 AA. AC A0A0Q2L993; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 08-JUN-2016, entry version 4. 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:KQH72977.1}; GN ORFNames=AOT81_10935 {ECO:0000313|EMBL:KQH72977.1}; OS Xylella fastidiosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=2371 {ECO:0000313|EMBL:KQH72977.1, ECO:0000313|Proteomes:UP000051940}; RN [1] {ECO:0000313|EMBL:KQH72977.1, ECO:0000313|Proteomes:UP000051940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CO33 {ECO:0000313|EMBL:KQH72977.1, RC ECO:0000313|Proteomes:UP000051940}; RA Giampetruzzi A., Saponari M., Loconsole G., Martelli G.P., RA Chiumenti M., Boscia D., Saldarelli P., Calzolari A., Almeida R.; RT "Draft Genome Sequence of Xylella Fastidiosa CO33 Strain."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the thermodynamically favored C-C bond CC cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and CC succinate. {ECO:0000256|RuleBase:RU361121}. CC -!- FUNCTION: Involved in the catabolism of short chain fatty acids CC (SCFA) via the 2-methylcitrate cycle (propionate degradation CC route). Catalyzes the thermodynamically favored C-C bond cleavage CC of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate via CC an alpha-carboxy-carbanion intermediate. {ECO:0000256|HAMAP- CC Rule:MF_01939}. CC -!- CATALYTIC ACTIVITY: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = CC pyruvate + succinate. {ECO:0000256|HAMAP-Rule:MF_01939, CC ECO:0000256|RuleBase:RU361121}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC 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 CC superfamily. Methylisocitrate lyase family. {ECO:0000256|HAMAP- CC Rule:MF_01939, ECO:0000256|RuleBase:RU361121}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQH72977.1}. 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; LJZW01000024; KQH72977.1; -; Genomic_DNA. DR RefSeq; WP_057683671.1; NZ_LJZW01000024.1. DR Proteomes; UP000051940; Unassembled WGS sequence. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.60; -; 1. DR HAMAP; MF_01939; PrpB; 1. DR InterPro; IPR018523; Isocitrate_lyase_ph_CS. DR InterPro; IPR012695; PrpB. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR SUPFAM; SSF51621; SSF51621; 1. DR TIGRFAMs; TIGR02317; prpB; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051940}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01939, ECO:0000256|RuleBase:RU361121, KW ECO:0000313|EMBL:KQH72977.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01939}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01939}. FT REGION 49 51 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT REGION 127 128 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT REGION 214 216 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT METAL 89 89 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01939}. FT METAL 91 91 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01939}. FT BINDING 162 162 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01939}. FT BINDING 192 192 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01939}. FT BINDING 245 245 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01939}. FT BINDING 274 274 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01939}. SQ SEQUENCE 298 AA; 32455 MW; 0A91610DCDB26E45 CRC64; MSTSLPIQTP GQCFRTALMN ERPLQVIGAM NAYHALLAQR AGYRALYLSG GGVAAGSLGL PDLGINTLED VLIDVRRITD VCDLPLLVDI DTGFGPSALN IERTIKTLIK AGAAACHIED QVAAKRCGHR PGKEIVSLSD MADRVKAAAD ARTDATFFLI ARTDAIQAEG VEVAIERAQA YVEAGADSIF AEAVSDLETY RHFVERIRVP VLANMTEFGK TPLLTREQLE AVGVAMQLFP LSAFRAANKA AETVYMAIRR DGHQQAVLPH MQTRAELYER LDYHAFEQRL DALSSRST //