(data stored in ACNUC7421 zone)

SWISSPROT: B2UHC4_RALPJ

ID   B2UHC4_RALPJ            Unreviewed;       298 AA.
AC   B2UHC4;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=2-methylisocitrate lyase {ECO:0000256|HAMAP-Rule:MF_01939};
DE            Short=2-MIC {ECO:0000256|HAMAP-Rule:MF_01939};
DE            Short=MICL {ECO:0000256|HAMAP-Rule:MF_01939};
DE            EC=4.1.3.30 {ECO:0000256|HAMAP-Rule:MF_01939};
DE   AltName: Full=(2R,3S)-2-methylisocitrate lyase {ECO:0000256|HAMAP-Rule:MF_01939};
GN   Name=prpB {ECO:0000256|HAMAP-Rule:MF_01939};
GN   OrderedLocusNames=Rpic_3861 {ECO:0000313|EMBL:ACD28975.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD28975.1, ECO:0000313|Proteomes:UP000002566};
RN   [1] {ECO:0000313|Proteomes:UP000002566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the thermodynamically favored C-C bond
CC       cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and
CC       succinate. {ECO:0000256|RuleBase:RU361121}.
CC   -!- FUNCTION: Involved in the catabolism of short chain fatty acids
CC       (SCFA) via the 2-methylcitrate cycle (propionate degradation
CC       route). Catalyzes the thermodynamically favored C-C bond cleavage
CC       of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate via
CC       an alpha-carboxy-carbanion intermediate. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01939,
CC         ECO:0000256|RuleBase:RU361121};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01939};
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000256|HAMAP-Rule:MF_01939, ECO:0000256|RuleBase:RU361121}.
CC   -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000256|HAMAP-
CC       Rule:MF_01939}.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase
CC       superfamily. Methylisocitrate lyase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01939, ECO:0000256|RuleBase:RU361121}.
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DR   EMBL; CP001069; ACD28975.1; -; Genomic_DNA.
DR   RefSeq; WP_012430019.1; NC_010678.1.
DR   STRING; 402626.Rpic_3861; -.
DR   EnsemblBacteria; ACD28975; ACD28975; Rpic_3861.
DR   GeneID; 6284964; -.
DR   KEGG; rpi:Rpic_3861; -.
DR   PATRIC; fig|402626.5.peg.103; -.
DR   eggNOG; ENOG4105CR4; Bacteria.
DR   eggNOG; COG2513; LUCA.
DR   HOGENOM; HOG000220041; -.
DR   KO; K03417; -.
DR   OMA; AHACSYD; -.
DR   OrthoDB; 1485205at2; -.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000002566; Chromosome 2.
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;
DR   PRODOM; B2UHC4.
DR   SWISS-2DPAGE; B2UHC4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01939, ECO:0000256|RuleBase:RU361121,
KW   ECO:0000313|EMBL:ACD28975.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01939};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01939};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002566}.
FT   REGION       50     52       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01939}.
FT   REGION      127    128       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01939}.
FT   REGION      214    216       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01939}.
FT   METAL        90     90       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01939}.
FT   METAL        92     92       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01939}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01939}.
FT   BINDING     192    192       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01939}.
FT   BINDING     245    245       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01939}.
FT   BINDING     274    274       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01939}.
SQ   SEQUENCE   298 AA;  32092 MW;  4464514E34AF1FFF CRC64;
     MSTTHRHPTS AGAKFRAAVA ESQPLQVVGA ITAYAAKMAE QTGFKAVYLS GGGVAANSLG
     IPDLGISTME DVLIDARRIT DAVQIPLMVD IDTGWGGAFN IARTIRSFIK AGVAAVHLED
     QVGQKRCGHR PGKEVVSTDE MVDRVKAAVD ARTDDDFVIM ARTDAAASEG IDAAIERAVA
     YVEAGADMIF PEAMKTLDDY RRFKAAVKVP ILANLTEFGS TPLFTTDELR SANVDIALYC
     CGAYRAMNAA ALNFYQTVMR DGTQKAAVET MQSRADLYQY LGYHAYEDKL DALFAAKK
//

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