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TPDB1_COMSP
ID   TPDB1_COMSP             Reviewed;         154 AA.
AC   Q3C1E2;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Terephthalate 1,2-dioxygenase, terminal oxygenase component subunit beta 1;
DE            Short=TPADO terminal oxygenase component;
DE            EC=1.14.12.15 {ECO:0000269|PubMed:18776687};
DE   AltName: Full=TER dioxygenase system;
DE            Short=TERDOS;
DE   AltName: Full=Terephthalate 1,2-dioxygenase small subunit 1;
GN   Name=tphA3I;
OS   Comamonas sp.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas; unclassified Comamonas.
OX   NCBI_TaxID=34028;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A TEREPHTHALATE DIOXYGENASE,
RP   FUNCTION IN TPA DEGRADATION, SUBUNIT, AND COFACTOR.
RC   STRAIN=E6;
RX   PubMed=16517628; DOI=10.1128/aem.72.3.1825-1832.2006;
RA   Sasoh M., Masai E., Ishibashi S., Hara H., Kamimura N., Miyauchi K.,
RA   Fukuda M.;
RT   "Characterization of the terephthalate degradation genes of Comamonas sp.
RT   strain E6.";
RL   Appl. Environ. Microbiol. 72:1825-1832(2006).
RN   [2]
RP   FUNCTION AS A TEREPHTHALATE DIOXYGENASE, SUBSTRATE SPECIFICITY, COFACTOR,
RP   AND SUBUNIT.
RC   STRAIN=E6;
RX   PubMed=7961417; DOI=10.1128/jb.176.21.6644-6652.1994;
RA   Schlafli H.R., Weiss M.A., Leisinger T., Cook A.M.;
RT   "Terephthalate 1,2-dioxygenase system from Comamonas testosteroni T-2:
RT   purification and some properties of the oxygenase component.";
RL   J. Bacteriol. 176:6644-6652(1994).
RN   [3]
RP   FUNCTION AS A TEREPHTHALATE DIOXYGENASE, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, AND SUBSTRATE
RP   SPECIFICITY.
RC   STRAIN=E6;
RX   PubMed=18776687; DOI=10.1271/bbb.80236;
RA   Fukuhara Y., Kasai D., Katayama Y., Fukuda M., Masai E.;
RT   "Enzymatic properties of terephthalate 1,2-dioxygenase of Comamonas sp.
RT   strain E6.";
RL   Biosci. Biotechnol. Biochem. 72:2335-2341(2008).
CC   -!- FUNCTION: Component of the terephthalate 1,2-dioxygenase multicomponent
CC       enzyme system which catalyzes the dioxygenation of terephthalate
CC       (TER/TPA) to 1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylic acid
CC       (DCD). It can also use 2,5-dicarboxypyridine (PDC) and 1,4-
CC       napthalenedicarboxylic acid (NDC) as substrates, and preferentially
CC       uses NADPH which is the physiological electron donor.
CC       {ECO:0000269|PubMed:16517628, ECO:0000269|PubMed:18776687,
CC       ECO:0000269|PubMed:7961417}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADH + O2 + terephthalate = (3S,4R)-3,4-
CC         dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate + NAD(+);
CC         Xref=Rhea:RHEA:10312, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:30043, ChEBI:CHEBI:57412, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.14.12.15;
CC         Evidence={ECO:0000269|PubMed:18776687};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000269|PubMed:16517628, ECO:0000269|PubMed:18776687,
CC         ECO:0000269|PubMed:7961417};
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:18776687}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=72 uM for TPA (at 30 degrees Celsius and at ph 7)
CC         {ECO:0000269|PubMed:18776687};
CC         Vmax=9.87 umol/min/mg enzyme with TPA as substrate (at 30 degrees
CC         Celsius and at ph 7) {ECO:0000269|PubMed:18776687};
CC       pH dependence:
CC         Optimum pH is 7. About 20% of maximum TPADO activity is observed at
CC         pH 9, whereas no activity is observed at pH 5.
CC         {ECO:0000269|PubMed:18776687};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius. Approximately 60% of
CC         maximum TPADO activity is observed at 15 degrees Celsius, and
CC         activity is completely lost at 50 degrees Celsius.
CC         {ECO:0000269|PubMed:18776687};
CC   -!- SUBUNIT: Heterotetramer composed of 2 alpha (TphA2I and TphA2II) and 2
CC       beta (TphA3I and TphA3II) subunits (Probable). Part of a multicomponent
CC       enzyme system composed of a reductase (TphA1I or TphA1II) and a two-
CC       subunit oxygenase component (TphA2I or TphA2II and TphA3I or TphA3II).
CC       {ECO:0000269|PubMed:16517628, ECO:0000269|PubMed:7961417, ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       beta subunit family. {ECO:0000305}.
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DR   EMBL; AB238678; BAE47078.1; -; Genomic_DNA.
DR   PDB; 7Q04; X-ray; 2.28 A; A/B/C=1-154.
DR   PDB; 7Q05; X-ray; 2.08 A; A/B/C=1-154.
DR   PDB; 7Q06; X-ray; 1.95 A; A/B/C=1-154.
DR   PDBsum; 7Q04; -.
DR   PDBsum; 7Q05; -.
DR   PDBsum; 7Q06; -.
DR   AlphaFoldDB; Q3C1E2; -.
DR   SMR; Q3C1E2; -.
DR   GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR   GO; GO:0018628; F:terephthalate 1,2-dioxygenase activity; IDA:UniProtKB.
DR   GO; GO:0018963; P:phthalate metabolic process; IDA:UniProtKB.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR000391; Rng_hydr_dOase-bsu.
DR   Pfam; PF00866; Ring_hydroxyl_B; 1.
DR   SUPFAM; SSF54427; SSF54427; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Dioxygenase; NAD; Oxidoreductase.
FT   CHAIN           1..154
FT                   /note="Terephthalate 1,2-dioxygenase, terminal oxygenase
FT                   component subunit beta 1"
FT                   /id="PRO_0000419004"
SQ   SEQUENCE   154 AA;  17231 MW;  16074C1EF7A7E3EF CRC64;
     MINEIQIAAF NAAYAKTVDS DAMEQWPTFF TKDCHYRVTN VDNHAEGLAA GIVWADSQDM
     LTDRISALRE ANIYERHRYR HILGLPSIQS GDATQASAST PFMVLRIMHT GETEVFASGE
     YLDKFTTIDG KLRLQERIAV CDSTVTDTLM ALPL
 
 
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