(data stored in SCRATCH zone)

SWISSPROT: C0ZL91_RHOE4

ID   C0ZL91_RHOE4            Unreviewed;       158 AA.
AC   C0ZL91;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=4-hydroxy-4-methyl-2-oxoglutarate aldolase {ECO:0000256|RuleBase:RU004338, ECO:0000256|SAAS:SAAS00851321};
DE            Short=HMG aldolase {ECO:0000256|RuleBase:RU004338};
DE            EC=4.1.1.112 {ECO:0000256|RuleBase:RU004338};
DE            EC=4.1.3.17 {ECO:0000256|RuleBase:RU004338, ECO:0000256|SAAS:SAAS00851321};
DE   AltName: Full=Oxaloacetate decarboxylase {ECO:0000256|RuleBase:RU004338};
GN   Name=rraA {ECO:0000313|EMBL:BAH30781.1};
GN   OrderedLocusNames=RER_00730 {ECO:0000313|EMBL:BAH30781.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH30781.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH30781.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus
RT   erythropolis strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
CC   -!- FUNCTION: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-
CC       oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a
CC       secondary oxaloacetate (OAA) decarboxylase activity due to the
CC       common pyruvate enolate transition state formed following C-C bond
CC       cleavage in the retro-aldol and decarboxylation reactions.
CC       {ECO:0000256|RuleBase:RU004338, ECO:0000256|SAAS:SAAS00851326}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate;
CC         Xref=Rhea:RHEA:22748, ChEBI:CHEBI:15361, ChEBI:CHEBI:58276;
CC         EC=4.1.3.17; Evidence={ECO:0000256|RuleBase:RU004338,
CC         ECO:0000256|SAAS:SAAS01115624};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + oxaloacetate = CO2 + pyruvate;
CC         Xref=Rhea:RHEA:15641, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:16526; EC=4.1.1.112;
CC         Evidence={ECO:0000256|RuleBase:RU004338,
CC         ECO:0000256|SAAS:SAAS01115623};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|RuleBase:RU004338,
CC         ECO:0000256|SAAS:SAAS00851318};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|RuleBase:RU004338,
CC       ECO:0000256|SAAS:SAAS00851327}.
CC   -!- SIMILARITY: Belongs to the class II aldolase/RraA-like family.
CC       {ECO:0000256|RuleBase:RU004338, ECO:0000256|SAAS:SAAS00851328}.
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DR   EMBL; AP008957; BAH30781.1; -; Genomic_DNA.
DR   RefSeq; WP_003943552.1; NC_012490.1.
DR   STRING; 234621.RER_00730; -.
DR   EnsemblBacteria; BAH30781; BAH30781; RER_00730.
DR   GeneID; 31539948; -.
DR   KEGG; rer:RER_00730; -.
DR   PATRIC; fig|234621.6.peg.502; -.
DR   eggNOG; ENOG4108YYX; Bacteria.
DR   eggNOG; COG0684; LUCA.
DR   HOGENOM; HOG000252803; -.
DR   KO; K02553; -.
DR   OMA; RSCDTQF; -.
DR   Proteomes; UP000002204; Chromosome.
DR   GO; GO:0047443; F:4-hydroxy-4-methyl-2-oxoglutarate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008428; F:ribonuclease inhibitor activity; IEA:InterPro.
DR   GO; GO:0051252; P:regulation of RNA metabolic process; IEA:InterPro.
DR   CDD; cd16841; RraA_family; 1.
DR   InterPro; IPR010203; RraA.
DR   InterPro; IPR005493; RraA/RraA-like.
DR   InterPro; IPR036704; RraA/RraA-like_sf.
DR   Pfam; PF03737; RraA-like; 1.
DR   SUPFAM; SSF89562; SSF89562; 1.
DR   TIGRFAMs; TIGR01935; NOT-MenG; 1.
PE   3: Inferred from homology;
DR   PRODOM; C0ZL91.
DR   SWISS-2DPAGE; C0ZL91.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002204};
KW   Lyase {ECO:0000256|RuleBase:RU004338, ECO:0000256|SAAS:SAAS00851323};
KW   Metal-binding {ECO:0000256|RuleBase:RU004338,
KW   ECO:0000256|SAAS:SAAS00851319}.
SQ   SEQUENCE   158 AA;  16410 MW;  024688DA1BDEFB4B CRC64;
     MTEPVATADL ADEIGPDIRS CDTQFTQFGG REVFAGPITT IKCFQDNLLV KQTLSEPGNG
     GVLVVDGDAS IHTALVGDII AGRGVDNGWA GVIVNGAVRD SAILRTLDIG VKALGTNPRK
     STQTGSGEKN VPIEIGGVTF NPGEIVYSDQ DGVVVRES
//

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