位置:首页 > 蛋白库 > PHDJ_NOCSK
PHDJ_NOCSK
ID   PHDJ_NOCSK              Reviewed;         332 AA.
AC   Q79EM8; O24722;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Trans-2'-carboxybenzalpyruvate hydratase-aldolase {ECO:0000312|EMBL:BAA24966.1};
DE            EC=4.1.2.34;
GN   Name=phdJ {ECO:0000312|EMBL:BAA24966.1};
OS   Nocardioides sp. (strain KP7).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=102632;
RN   [1] {ECO:0000312|EMBL:BAA23263.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9335300; DOI=10.1128/jb.179.20.6488-6494.1997;
RA   Iwabuchi T., Harayama S.;
RT   "Biochemical and genetic characterization of 2-carboxybenzaldehyde
RT   dehydrogenase, an enzyme involved in phenanthrene degradation by
RT   Nocardioides sp. strain KP7.";
RL   J. Bacteriol. 179:6488-6494(1997).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:BAA24966.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-25, FUNCTION,
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBUNIT, AND INDUCTION.
RX   PubMed=9473051; DOI=10.1128/jb.180.4.945-949.1998;
RA   Iwabuchi T., Harayama S.;
RT   "Biochemical and genetic characterization of trans-2'-carboxybenzalpyruvate
RT   hydratase-aldolase from a phenanthrene-degrading Nocardioides strain.";
RL   J. Bacteriol. 180:945-949(1998).
CC   -!- FUNCTION: Plays a role in phenanthrene catabolism. Catalyzes the
CC       transformation of trans-2'-carboxbenzalpyruvate to 2-formylbenzoate and
CC       pyruvate. {ECO:0000269|PubMed:9473051}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate + H2O = 2-
CC         formylbenzoate + pyruvate; Xref=Rhea:RHEA:16453, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:58203, ChEBI:CHEBI:58794; EC=4.1.2.34;
CC         Evidence={ECO:0000269|PubMed:9473051};
CC   -!- ACTIVITY REGULATION: Not inhibited by sodium borohydride or sodium
CC       pyruvate. Unaffected by EDTA, EGTA, Mn(2+), Mg(2+) and Ca(2+).
CC       {ECO:0000269|PubMed:9473051}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=50 uM for trans-2'-carboxbenzalpyruvate
CC         {ECO:0000269|PubMed:9473051};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:9473051};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:9473051};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:9473051}.
CC   -!- INDUCTION: By phenanthrene. {ECO:0000269|PubMed:9473051}.
CC   -!- SIMILARITY: Belongs to the DapA family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB000735; BAA23263.1; -; Genomic_DNA.
DR   EMBL; D89988; BAA24966.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q79EM8; -.
DR   SMR; Q79EM8; -.
DR   BRENDA; 4.1.2.34; 4363.
DR   GO; GO:0018803; F:4-(2-carboxyphenyl)-2-oxobut-3-enoate aldolase activity; IDA:UniProtKB.
DR   GO; GO:0042216; P:phenanthrene catabolic process; IDA:UniProtKB.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   PANTHER; PTHR12128; PTHR12128; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Direct protein sequencing; Lyase;
KW   Pyruvate.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9473051"
FT   CHAIN           2..332
FT                   /note="Trans-2'-carboxybenzalpyruvate hydratase-aldolase"
FT                   /evidence="ECO:0000269|PubMed:9473051"
FT                   /id="PRO_0000403697"
FT   ACT_SITE        178
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            150
FT                   /note="Involved in proton transfer during cleavage"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   332 AA;  34881 MW;  59E9210E35BE1E0C CRC64;
     MTSPAVTSAD ITGLVGIVPT PSKPGSEAPD AVDTVDLDET ARMVELIVAS GVDVLLTNGT
     FGEVATLTYE ELLAFNDTVI RTVANRIPVF CGASTLNTRD TIARSLALMG LGANGLFVGR
     PMWLPLDDEQ LVSYYAAVCD AVPAAAVVVY DNTGVFKGKI SSAAYAALAE IPQIVASKHL
     GVLSGSDAYA SDLAAVKGRF PLLPTADNWL PSLEAFPGEV PAAWSGDVAC GPEPVMALRR
     AIAEGLWDDA RAVHEDIAWA TEPLFPGGDI SKFMPYSIQI DRAEFEAAGY IVPGPSRHPY
     GTAPAAYLEG GAEVGRRWAG IRQKYVATLA EP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024