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 24-JAN-2024, entry version 44.
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; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; 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}.
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; 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 Gene3D; 3.10.450.50; -; 1.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR037401; SnoaL-like.
DR Pfam; PF13577; SnoaL_4; 1.
DR SUPFAM; SSF54427; NTF2-like; 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"
FT HELIX 4..19
FT /evidence="ECO:0007829|PDB:7Q06"
FT HELIX 23..29
FT /evidence="ECO:0007829|PDB:7Q06"
FT STRAND 30..40
FT /evidence="ECO:0007829|PDB:7Q06"
FT HELIX 41..46
FT /evidence="ECO:0007829|PDB:7Q06"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:7Q06"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:7Q06"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:7Q06"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:7Q06"
FT STRAND 96..108
FT /evidence="ECO:0007829|PDB:7Q06"
FT STRAND 113..128
FT /evidence="ECO:0007829|PDB:7Q06"
FT STRAND 131..142
FT /evidence="ECO:0007829|PDB:7Q06"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:7Q06"
SQ SEQUENCE 154 AA; 17231 MW; 16074C1EF7A7E3EF CRC64;
MINEIQIAAF NAAYAKTVDS DAMEQWPTFF TKDCHYRVTN VDNHAEGLAA GIVWADSQDM
LTDRISALRE ANIYERHRYR HILGLPSIQS GDATQASAST PFMVLRIMHT GETEVFASGE
YLDKFTTIDG KLRLQERIAV CDSTVTDTLM ALPL
//
