PRPB_VIBCH
ID PRPB_VIBCH Reviewed; 308 AA.
AC Q9KSC2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=2-methylisocitrate lyase {ECO:0000255|HAMAP-Rule:MF_01939};
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=prpB {ECO:0000255|HAMAP-Rule:MF_01939}; OrderedLocusNames=VC_1336;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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 reaction of
CC (2R,3S)-2-methylisocitrate to yield pyruvate and succinate via an
CC alpha-carboxy-carbanion intermediate. {ECO:0000255|HAMAP-
CC Rule:MF_01939}.
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 -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000255|HAMAP-Rule:MF_01939}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_01939}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Methylisocitrate lyase family. {ECO:0000255|HAMAP-Rule:MF_01939}.
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DR EMBL; AE003852; AAF94494.1; -; Genomic_DNA.
DR PIR; H82212; H82212.
DR RefSeq; NP_230980.1; NC_002505.1.
DR AlphaFoldDB; Q9KSC2; -.
DR SMR; Q9KSC2; -.
DR STRING; 243277.VC_1336; -.
DR DNASU; 2614790; -.
DR EnsemblBacteria; AAF94494; AAF94494; VC_1336.
DR KEGG; vch:VC_1336; -.
DR PATRIC; fig|243277.26.peg.1273; -.
DR eggNOG; COG2513; Bacteria.
DR HOGENOM; CLU_027389_3_2_6; -.
DR OMA; QTELWNK; -.
DR BioCyc; VCHO:VC1336-MON; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IBA:GO_Central.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IBA:GO_Central.
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..308
FT /note="2-methylisocitrate lyase"
FT /id="PRO_0000068817"
FT BINDING 54..56
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 131..132
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 224..226
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
SQ SEQUENCE 308 AA; 33737 MW; FFD0161D61ACAA52 CRC64;
MPNNKVKENP MSLSPGAKFR LAVKTHHPLQ IVGTINPYCA MMAKSIGHQA IYLSGGGIAN
ASYGLPDLGI TTLNDVLVDV ERITNACDLP LLVDIDTGFG GAFNIARTIK AMEKAGAAAV
HMEDQVAQKR CGHRPNKAIV SQQEMVDRVK AAVDARINPE FVIMARTDAL AVEGMDSAIE
RAIACVEAGA DMIFPEAMTE LKQYEQFSTA LRSATGKPVP ILANITEFGQ TPLYSGEQLA
AVNVDMVLYP LSAFRAMNKA AENVYRHLLE HGNQEALLDQ MQTRKELYAY LHYHEYEDKL
DQLFSQPS
