ID A0A2N0ZMP7_9BACI Unreviewed; 301 AA.
AC A0A2N0ZMP7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:PKG30773.1};
GN ORFNames=CWS20_01460 {ECO:0000313|EMBL:PKG30773.1};
OS Cytobacillus horneckiae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Cytobacillus.
OX NCBI_TaxID=549687 {ECO:0000313|EMBL:PKG30773.1, ECO:0000313|Proteomes:UP000233343};
RN [1] {ECO:0000313|EMBL:PKG30773.1, ECO:0000313|Proteomes:UP000233343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1PO1SC {ECO:0000313|Proteomes:UP000233343};
RX PubMed=19666815; DOI=10.1099/ijs.0.008979-0;
RA Vaishampayan P., Probst A., Krishnamurthi S., Ghosh S., Osman S.,
RA McDowall A., Ruckmani A., Mayilraj S., Venkateswaran K.;
RT "Bacillus horneckiae sp. nov., isolated from a spacecraft-assembly clean
RT room.";
RL Int. J. Syst. Evol. Microbiol. 60:1031-1037(2010).
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:PKG30773.1}.
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DR EMBL; PISD01000005; PKG30773.1; -; Genomic_DNA.
DR RefSeq; WP_066193661.1; NZ_PISD01000005.1.
DR AlphaFoldDB; A0A2N0ZMP7; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000233343; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU361121, ECO:0000313|EMBL:PKG30773.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233343}.
SQ SEQUENCE 301 AA; 33035 MW; BC262613C03714DE CRC64;
MAWIVDKAKT QLELAQRFSE LVSSPPILQI PGAHDAMAAL VAQKAGFLAL YLSGAAYTAS
RGLPDLGIVT SSELAERAKD IVRATNLPLL VDIDTGFGGV LNAARTAVEM EEAKVAAVQV
EDQQLPKKCG HLNGKQLVTI EEMVQKIKVM KEAAPTLYIV ARTDARAVEG LEASIKRAEA
YLEAGADAIF PEALQSAEEF RLFSERVAVP LLANMTEFGK TPYYSAEEFS EMGFQMVIYP
VTSLRVAAKA YEQVFDLIKT TGTQKDALAA MQTRKELYET ISYFKFEDLD RELAKTILEK
E
//
