ID   A0A6L7HJ56_BACAN        Unreviewed;       302 AA.
AC   A0A6L7HJ56; A0A0F7RI56; E9R2D6; E9R2D7; Q6HYY7; Q6KSY6; Q81QR8;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   27-MAR-2024, entry version 16.
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:AAT31469.1};
GN   OrderedLocusNames=GBAA_2350 {ECO:0000313|EMBL:AAT31469.1};
OS   Bacillus anthracis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392 {ECO:0000313|EMBL:AAT31469.1, ECO:0000313|Proteomes:UP000000594};
RN   [1] {ECO:0000313|EMBL:AAT31469.1, ECO:0000313|Proteomes:UP000000594}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor {ECO:0000313|Proteomes:UP000000594};
RX   PubMed=18952800; DOI=10.1128/JB.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
RN   [2] {ECO:0007829|PDB:4IQE}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
RG   Center for Structural Genomics of Infectious Diseases (CSGID);
RA   Kim Y., Maltseva N., Kwon K., Anderson W.F., Joachimiak A.;
RT   "Crystal Structure of Carboxyvinyl-Carboxyphosphonate Phosphorylmutase from
RT   Bacillus anthracis str. Ames Ancestor.";
RL   Submitted (JAN-2013) to the PDB data bank.
RN   [3] {ECO:0007829|PDB:4IQD}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH PYRUVATE.
RG   Center for Structural Genomics of Infectious Diseases (CSGID);
RA   Kim Y., Maltseva N., Kwon K., Anderson W.F., Joachimiak A.;
RT   "Crystal Structure of Carboxyvinyl-Carboxyphosphonate Phosphorylmutase from
RT   Bacillus anthracis.";
RL   Submitted (JAN-2013) to the PDB data bank.
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}.
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DR   EMBL; AE017334; AAT31469.1; -; Genomic_DNA.
DR   RefSeq; WP_000312652.1; NZ_WXXJ01000007.1.
DR   PDB; 4IQD; X-ray; 2.00 A; A/B=1-302.
DR   PDB; 4IQE; X-ray; 2.50 A; A/B=1-302.
DR   AlphaFoldDB; A0A6L7HJ56; -.
DR   SMR; A0A6L7HJ56; -.
DR   GeneID; 45022232; -.
DR   KEGG; bar:GBAA_2350; -.
DR   PATRIC; fig|1392.230.peg.2308; -.
DR   OMA; YDFLNYH; -.
DR   OrthoDB; 8629576at2; -.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000000594; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4IQD, ECO:0007829|PDB:4IQE};
KW   Lyase {ECO:0000256|RuleBase:RU361121, ECO:0000313|EMBL:AAT31469.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000594}.
FT   BINDING         53
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:4IQD"
FT   BINDING         77
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:4IQD"
FT   BINDING         119
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:4IQD"
FT   BINDING         162
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:4IQD"
SQ   SEQUENCE   302 AA;  33016 MW;  FFCD10E8A9CB1F7B CRC64;
     MAWVVNKQST QEELANRFRA LVEANEILQI PGAHDAMAAL VARNTGFLAL YLSGAAYTAS
     KGLPDLGIVT STEVAERARD LVRATDLPVL VDIDTGFGGV LNVARTAVEM VEAKVAAVQI
     EDQQLPKKCG HLNGKKLVTT EELVQKIKAI KEVAPSLYIV ARTDARGVEG LDEAIERANA
     YVKAGADAIF PEALQSEEEF RLFNSKVNAP LLANMTEFGK TPYYSAEEFA NMGFQMVIYP
     VTSLRVAAKA YENVFTLIKE TGSQKDALSN MQTRSELYET ISYHDFEELD TGIAKTVLSE
     DQ
//