PRPB2_CORGL
ID PRPB2_CORGL Reviewed; 307 AA.
AC Q8NSL2;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable 2-methylisocitrate lyase 2 {ECO:0000305};
DE Short=2-MIC {ECO:0000305};
DE Short=MICL {ECO:0000305};
DE EC=4.1.3.30 {ECO:0000250|UniProtKB:P77541};
DE AltName: Full=(2R,3S)-2-methylisocitrate lyase {ECO:0000250|UniProtKB:P77541};
GN Name=prpB2 {ECO:0000305}; OrderedLocusNames=Cgl0658, cg0760;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=11976302; DOI=10.1128/jb.184.10.2728-2739.2002;
RA Claes W.A., Puehler A., Kalinowski J.;
RT "Identification of two prpDBC gene clusters in Corynebacterium glutamicum
RT and their involvement in propionate degradation via the 2-methylcitrate
RT cycle.";
RL J. Bacteriol. 184:2728-2739(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
CC -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the 2-methylcitrate cycle I (propionate degradation route).
CC Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-
CC methylisocitrate to yield pyruvate and succinate via an alpha-carboxy-
CC carbanion intermediate. {ECO:0000269|PubMed:11976302}.
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:0000250|UniProtKB:P77541};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P77541};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000250|UniProtKB:P77541}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000250|UniProtKB:P77541}.
CC -!- MISCELLANEOUS: The prpD2B2C2 operon is essential for growth on
CC propionate as sole carbon source. {ECO:0000269|PubMed:11976302}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Methylisocitrate lyase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB98051.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF434799; AAM21505.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98051.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX927149; CAF19364.1; -; Genomic_DNA.
DR RefSeq; NP_599890.2; NC_003450.3.
DR RefSeq; WP_011265603.1; NC_006958.1.
DR AlphaFoldDB; Q8NSL2; -.
DR SMR; Q8NSL2; -.
DR STRING; 196627.cg0760; -.
DR KEGG; cgb:cg0760; -.
DR KEGG; cgl:Cgl0658; -.
DR PATRIC; fig|196627.13.peg.644; -.
DR eggNOG; COG2513; Bacteria.
DR HOGENOM; CLU_027389_3_2_11; -.
DR OMA; VKDLAPW; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000000582; 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; -; 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 SUPFAM; SSF51621; SSF51621; 1.
DR TIGRFAMs; TIGR02317; prpB; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 3: Inferred from homology;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..307
FT /note="Probable 2-methylisocitrate lyase 2"
FT /id="PRO_0000068814"
FT BINDING 53..55
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77541"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P77541"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P77541"
FT BINDING 129..130
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77541"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77541"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77541"
FT BINDING 216..218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77541"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77541"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77541"
SQ SEQUENCE 307 AA; 33275 MW; 5BE10A43623A6FB3 CRC64;
MAGLFSSAVA PTERRKALRA ALAAPEIARM PGAFSPLAAR AIQEAGFEGV YVSGAVVAAD
LALPDIGLTT LTEVAHRSRQ IARVTDLPVL VDADTGFGEP MSAARTVSEL EDAGVAGCHL
EDQVNPKRCG HLDGKEVVGT DIMVRRIAAA VNERRDEQFV ICARTDAAGV EGIDSAIERA
KAYADAGADM IFTEALYSPA DFEKFRAAVD IPLLANMTEF GKTELLPAQL LEDIGYNAVI
YPVTLLRIAM GQVEQALGDI ANTGIQTDWV DRMQHRSRLY ELLRYNEYNA FDQQVFTYSA
DSYKPIF
