TPDA2_COMSP
ID TPDA2_COMSP Reviewed; 413 AA.
AC Q3C1D5;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Terephthalate 1,2-dioxygenase, terminal oxygenase component subunit alpha 2;
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 large subunit 2;
GN Name=tphA2II;
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 AND IN TPA DEGRADATION, AND DISRUPTION PHENOTYPE.
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 PROTEIN SEQUENCE OF 1-17, FUNCTION AS A TEREPHTHALATE DIOXYGENASE,
RP SUBSTRATE SPECIFICITY, COFACTOR, 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, COFACTOR, ACTIVITY REGULATION, SUBUNIT, AND
RP SUBSTRATE 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:18776687, ECO:0000269|PubMed:7961417};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
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. Part of a multicomponent enzyme
CC system composed of a reductase (TphA1I or TphA1II) and a two-subunit
CC oxygenase component (TphA2I or TphA2II and TphA3I or TphA3II).
CC {ECO:0000269|PubMed:18776687, ECO:0000269|PubMed:7961417}.
CC -!- DISRUPTION PHENOTYPE: Not affected by disruption of tphA2II, however
CC the tphA2I/tphA2II double mutant no longer grows on TPA.
CC {ECO:0000269|PubMed:16517628}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha 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; AB238679; BAE47085.1; -; Genomic_DNA.
DR PDB; 7Q04; X-ray; 2.28 A; D/E/F=1-413.
DR PDB; 7Q05; X-ray; 2.08 A; D/E/F=1-413.
DR PDB; 7Q06; X-ray; 1.95 A; D/E/F=1-413.
DR PDBsum; 7Q04; -.
DR PDBsum; 7Q05; -.
DR PDBsum; 7Q06; -.
DR AlphaFoldDB; Q3C1D5; -.
DR SMR; Q3C1D5; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
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 CDD; cd08880; RHO_alpha_C_ahdA1c-like; 1.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR043264; AhdA1c-like_alpha_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756; PTHR43756; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Dioxygenase; Direct protein sequencing; Iron;
KW Iron-sulfur; Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..413
FT /note="Terephthalate 1,2-dioxygenase, terminal oxygenase
FT component subunit alpha 2"
FT /id="PRO_0000419003"
FT DOMAIN 41..144
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 82
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 84
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 102
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 105
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 413 AA; 46243 MW; 79750780FF49640B CRC64;
MQESIIQWHG ATNTRVPFGI YTDTANADQE QQRIYRGEVW NYLCLESEIP GAGDFRTTFA
GETPIVVVRD ADQEIYAFEN RCAHRGALIA LEKSGRTDSF QCVYHAWSYN RQGDLTGVAF
EKGVKGQGGM PASFCKEEHG PRKLRVAVFC GLVFGSFSED VPSIEDYLGP EICERIERVL
HKPVEVIGRF TQKLPNNWKL YFENVKDSYH ASLLHMFFTT FELNRLSQKG GVIVDESGGH
HVSYSMIDRG AKDDSYKDQA IRSDNERYRL KDPSLLEGFE EFEDGVTLQI LSVFPGFVLQ
QIQNSIAVRQ LLPKSISSSE LNWTYLGYAD DSAEQRKVRL KQANLIGPAG FISMEDGAVG
GFVQRGIAGA ANLDAVIEMG GDHEGSSEGR ATETSVRGFW KAYRKHMGQE MQA
