PRPB_AERPE
ID PRPB_AERPE Reviewed; 308 AA.
AC Q9YFM7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 105.
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=APE_0222.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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 -!- 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; BA000002; BAA79134.2; -; Genomic_DNA.
DR PIR; D72779; D72779.
DR AlphaFoldDB; Q9YFM7; -.
DR SMR; Q9YFM7; -.
DR STRING; 272557.APE_0222.1; -.
DR EnsemblBacteria; BAA79134; BAA79134; APE_0222.1.
DR KEGG; ape:APE_0222.1; -.
DR PATRIC; fig|272557.25.peg.159; -.
DR eggNOG; arCOG00581; Archaea.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000002518; 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..308
FT /note="2-methylisocitrate lyase"
FT /id="PRO_0000068821"
FT BINDING 51..53
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 127..128
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 212..214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01939"
SQ SEQUENCE 308 AA; 34347 MW; B3023794C0829EDC CRC64;
MAFLYREPLE RPGLVLRELI EKRDIVVAPG VYNPAVALLA ERMGFEALYL SGAAITGSLA
MPDLGLITLS ELAMFTSYIT RVVRVPVIVD ADTGFGEAIN VERTVRELER AGAAAIQIED
QVMPKKCGHL QGKALISPED MVKKIIAAVG ARRDALIVAR TDARGVEGFE KAVERAQLYV
EAGADIIFPE ALTSLEEFRE FARRVKAPLL ANMTEFGKTP YITVDQFREA GYKIVIFPVT
TFRASLKASE TVLREIMEKG TQKDILDKLY TRTEFYDLIG YHDYEKRDAE VSRKAEELLA
RHNNSRTG
