ID A0A0Q9YU52_9COXI Unreviewed; 334 AA.
AC A0A0Q9YU52;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Methylisocitrate lyase {ECO:0000256|RuleBase:RU361121};
DE EC=4.1.3.30 {ECO:0000256|RuleBase:RU361121};
GN Name=prpB {ECO:0000313|EMBL:KRG20382.1};
GN ORFNames=HT99x_02478 {ECO:0000313|EMBL:KRG20382.1};
OS Candidatus Berkiella aquae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Berkiella.
OX NCBI_TaxID=295108 {ECO:0000313|EMBL:KRG20382.1, ECO:0000313|Proteomes:UP000051497};
RN [1] {ECO:0000313|EMBL:KRG20382.1, ECO:0000313|Proteomes:UP000051497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HT99 {ECO:0000313|EMBL:KRG20382.1,
RC ECO:0000313|Proteomes:UP000051497};
RA Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear
RT Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella
RT aquae.";
RL Submitted (SEP-2015) 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 -!- 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|RuleBase:RU361121};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000256|RuleBase:RU361121}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Methylisocitrate lyase family. {ECO:0000256|ARBA:ARBA00009282,
CC ECO:0000256|RuleBase:RU361121}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRG20382.1}.
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DR EMBL; LKAJ01000012; KRG20382.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q9YU52; -.
DR STRING; 295108.HT99x_02478; -.
DR PATRIC; fig|1590043.3.peg.2526; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000051497; Unassembled WGS sequence.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:InterPro.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 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|RuleBase:RU361121, ECO:0000313|EMBL:KRG20382.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051497}.
SQ SEQUENCE 334 AA; 36582 MW; 41E5CB89EF3BE8BD CRC64;
MHIQFVGYIT LADNSVVLRL PSGYNSLSAM VKKEILVLTE PGQLLRQAIQ TEKPLQIVGT
IHAYAARLAE ASGHKALYLS GAGVANSRLA LPDLAMTSLD DVVTEVTKIT QASTLPLLVD
ADTGWGSPLN IRRTFSMLSK AGAAGAHIED QTEAKRCGHR SGKKLVSTES MVGKIKAALD
GRNSDSFMVM ARTDAFAVEG LQGALERART YEAAGADAIF VEALDSLDHY LQFTRALTIP
VLANITEFGK TPLFSRESLA KVGVSMILYP LSAFRAMNQA ALKVYEAILQ QGTQQSVIPL
MQTRDELYQY LQYENYEKEL DEYNQLMERE DANN
//
