ID A0A1Q4DM45_9GAMM Unreviewed; 294 AA. AC A0A1Q4DM45; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 07-JUN-2017, entry version 3. 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=BGO90_15565 {ECO:0000313|EMBL:OJY45437.1}; OS Legionella sp. 40-6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=1895903 {ECO:0000313|EMBL:OJY45437.1, ECO:0000313|Proteomes:UP000186293}; RN [1] {ECO:0000313|EMBL:OJY45437.1, ECO:0000313|Proteomes:UP000186293} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=40-6 {ECO:0000313|EMBL:OJY45437.1}; RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., RA Anantharaman K., Tringe S., Hettich R.L., Harrison S.T., RA Banfield J.F.; RT "Genome-resolved meta-omics ties microbial dynamics to process RT performance in biotechnology for thiocyanate degradation."; RL Submitted (SEP-2016) 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:OJY45437.1}. 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; MKVI01000146; OJY45437.1; -; Genomic_DNA. DR UniPathway; UPA00946; -. DR Proteomes; UP000186293; 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 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:UP000186293}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01939, ECO:0000256|RuleBase:RU361121, KW ECO:0000313|EMBL:OJY45437.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01939}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01939}; KW Reference proteome {ECO:0000313|Proteomes:UP000186293}. FT REGION 44 46 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT REGION 121 122 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT REGION 208 210 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT METAL 84 84 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01939}. FT METAL 86 86 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01939}. FT BINDING 156 156 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01939}. FT BINDING 186 186 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01939}. FT BINDING 239 239 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01939}. FT BINDING 268 268 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01939}. SQ SEQUENCE 294 AA; 32125 MW; 99F2C706A0C667BD CRC64; MSHSPGKKFR ELVSQAQPLQ VLGTINAYAA MLAEQAGAQA IYLSGAGVAN ASYGLPDLGM TSLAEVLEDV QRITAATSLP LLVDIDTGWG HAFNIARTIA LMEKNGVAAV HIEDQVVAKR CGHRPNKAIV SAAEMGDRIK AAVDARKNED FVIMARTDAY AVEGMQAAID RALLCVQLGA DMIFPEAMTT LEEYSHFTQA VQVPVLANIT EFGKTPLFSR EELAQAGVSL VLYPLSAFRA MAKAALTTYQ QIIQQGTQQH MVEHMQTRQE LYAVLGYHAY EEKLDQLMEE RNER //