PRPB_SHEON
ID PRPB_SHEON Reviewed; 292 AA.
AC Q8EJW1;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=2-methylisocitrate lyase {ECO:0000303|PubMed:14702315};
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=SO_0345;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
RN [2]
RP FUNCTION.
RC STRAIN=MR-1;
RX PubMed=14702315; DOI=10.1128/jb.186.2.454-462.2004;
RA Grimek T.L., Escalante-Semerena J.C.;
RT "The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a new
RT Fe/S-dependent 2-methylcitrate dehydratase enzyme that requires prpF
RT function in vivo.";
RL J. Bacteriol. 186:454-462(2004).
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:0000255|HAMAP-Rule:MF_01939,
CC ECO:0000269|PubMed:14702315}.
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; AE014299; AAN53430.1; -; Genomic_DNA.
DR RefSeq; NP_715985.1; NC_004347.2.
DR RefSeq; WP_011070710.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EJW1; -.
DR SMR; Q8EJW1; -.
DR STRING; 211586.SO_0345; -.
DR PaxDb; Q8EJW1; -.
DR KEGG; son:SO_0345; -.
DR PATRIC; fig|211586.12.peg.335; -.
DR eggNOG; COG2513; Bacteria.
DR HOGENOM; CLU_027389_3_2_6; -.
DR OMA; QTELWNK; -.
DR OrthoDB; 1485205at2; -.
DR PhylomeDB; Q8EJW1; -.
DR BioCyc; SONE211586:G1GMP-330-MON; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IDA:UniProtKB.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; ISS:UniProtKB.
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..292
FT /note="2-methylisocitrate lyase"
FT /id="PRO_0000432932"
FT BINDING 44..46
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 121..122
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 208..210
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
SQ SEQUENCE 292 AA; 31908 MW; CAF3A52358268DEF CRC64;
MTQSAGLRFR QALANSKPLQ IVGTTNAYFA LMAEQTGFQA LYLSGAGVAN ASYGLPDLGM
TSMNDVLIDA GRITSATQLP LLVDIDTGWG GAFNIARTIK EFEKIGVAAV HMEDQVSQKR
CGHRPNKAVV STEEMVDRIK AAVDARTDPN FVIMARTDAV AVEGLEAGIE RAKAYIAAGA
DMIFAEALTE LDQYRHFKAQ VKAPILANMT EFGQTQLFNK EELAQAGADM VLYPLGTFRA
ANQAALKVMQ ALMNDGHQRN VLDTMQTRAD LYKYLGYHAF EDKLDQLFSQ DK
