TPDR2_COMSP
ID TPDR2_COMSP Reviewed; 336 AA.
AC Q3C1D2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Terephthalate 1,2-dioxygenase, reductase component 2;
DE AltName: Full=TER dioxygenase system;
DE Short=TERDOS;
DE AltName: Full=TPADO reductase component;
DE EC=1.14.12.15 {ECO:0000269|PubMed:18776687};
GN Name=tphA1II;
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, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, AND
RP COFACTOR.
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). TphA1 probably reduces TphA2A3. It can also use 2,5-
CC dicarboxypyridine (PDC) and 1,4-napthalenedicarboxylic acid (NDC) as
CC substrates, and preferentially uses NADPH which is the physiological
CC electron donor. {ECO:0000269|PubMed:16517628,
CC ECO:0000269|PubMed:18776687}.
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=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC Note=Binds 1 FAD per subunit. {ECO:0000305};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000305};
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: Monomer. Part of a multicomponent enzyme system composed of a
CC reductase (TphA1I or TphA1II) and a two-subunit oxygenase component
CC (TphA2I or TphA2II and TphA3I or TphA3II).
CC {ECO:0000269|PubMed:16517628, ECO:0000269|PubMed:18776687}.
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DR EMBL; AB238679; BAE47088.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3C1D2; -.
DR SMR; Q3C1D2; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070402; F:NADPH 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 CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Dioxygenase; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..336
FT /note="Terephthalate 1,2-dioxygenase, reductase component
FT 2"
FT /id="PRO_0000419001"
FT DOMAIN 3..91
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 98..197
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 37
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305"
FT BINDING 42
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305"
FT BINDING 75
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 36340 MW; 43C6D87697426852 CRC64;
MNHQIHIHDS DIAFPCAPGQ SVLDAALQAG IELPYSCRKG SCGNCASTLL DGNIASFNGM
AVRNELCASE QVLLCGCTAA SDIRIHPSSF RRLDPEARKR FTAKVYSNTL AAPDVSLLRL
RLPVGKRAKF EAGQYLLIHL DDGESRSYSM ANPPHESDGI TLHVRHVPGG RFSTIVQQLK
SGDTLDIELP FGSIALKPDD ARPLICVAGG TGFAPIKSVL DDLAKRKVQR DITLIWGARN
PSGLYLPSAI DKWRKVWPQF RYIAAITDLG DMPADAHAGR VDDALRTHFG NLHDHVVHCC
GSPALVQSVR TAASDMGLLA QDFHADVFAT GPTGHH
