PRPB1_CORGL
ID PRPB1_CORGL Reviewed; 305 AA.
AC Q8NSH8;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable 2-methylisocitrate lyase 1 {ECO:0000303|PubMed:11976302};
DE Short=2-MIC {ECO:0000255|HAMAP-Rule:MF_01939};
DE Short=MICL {ECO:0000255|HAMAP-Rule:MF_01939};
DE EC=4.1.3.30 {ECO:0000255|HAMAP-Rule:MF_01939};
DE AltName: Full=(2R,3S)-2-methylisocitrate lyase {ECO:0000255|HAMAP-Rule:MF_01939};
GN Name=prpB1 {ECO:0000255|HAMAP-Rule:MF_01939};
GN OrderedLocusNames=Cgl0695, cg0797;
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: Catalyzes the thermodynamically favored C-C bond cleavage of
CC (2R,3S)-2-methylisocitrate to yield pyruvate and succinate via an
CC alpha-carboxy-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:0000255|HAMAP-Rule:MF_01939};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01939};
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_01939}.
CC -!- MISCELLANEOUS: The prpD1B1C1 operon seems not to be involved in
CC propionate degradation. {ECO:0000269|PubMed:11976302}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Methylisocitrate lyase family. {ECO:0000255|HAMAP-Rule:MF_01939}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB98088.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF434798; AAM21501.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98088.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX927150; CAF19400.1; -; Genomic_DNA.
DR RefSeq; NP_599927.1; NC_003450.3.
DR RefSeq; WP_011013822.1; NC_006958.1.
DR AlphaFoldDB; Q8NSH8; -.
DR SMR; Q8NSH8; -.
DR STRING; 196627.cg0797; -.
DR KEGG; cgb:cg0797; -.
DR KEGG; cgl:Cgl0695; -.
DR PATRIC; fig|196627.13.peg.681; -.
DR eggNOG; COG2513; Bacteria.
DR HOGENOM; CLU_027389_3_2_11; -.
DR OMA; QTELWNK; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:UniProtKB-UniRule.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR HAMAP; MF_01939; PrpB; 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..305
FT /note="Probable 2-methylisocitrate lyase 1"
FT /id="PRO_0000068813"
FT BINDING 52..54
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 128..129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 216..218
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
SQ SEQUENCE 305 AA; 33415 MW; 3BE9AEA72F2DA411 CRC64;
MNLFSNGVDV GRRRQAFKAA LAAPHIARLP GAFSPLIARS IEEAGFEGVY VSGAVIAADL
ALPDIGLTTL TEVAHRARQI ARVTDLGVLV DADTGFGEPM SAARTVAELE DAGVAGCHLE
DQVNPKRCGH LDGKEVVRTD VMVRRIAAAV SARRDPNFVI CARTDAAGVE GIDAAIERAK
AYLDAGADMI FTEALHSEAD FRYFRHAIPD ALLLANMTEF GKTTLLSADV LEEIGYNAVI
YPVTTLRIAM GQVEQALAEI KEHGTQEGWL DRMQHRSRLY ELLRYEDYNV FDQHIFTYRK
GENNE
