CARC_PSERE
ID CARC_PSERE Reviewed; 290 AA.
AC Q9AQM4; Q8GI17;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid hydrolase;
DE Short=HOPDA;
DE EC=3.7.1.13;
GN Name=carC;
OS Pseudomonas resinovorans.
OG Plasmid pCAR1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=53412;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBSTRATE SPECIFICITY, AND
RP NOMENCLATURE.
RC STRAIN=CA10;
RX PubMed=9244273; DOI=10.1128/jb.179.15.4841-4849.1997;
RA Sato S.I., Ouchiyama N., Kimura T., Nojiri H., Yamane H., Omori T.;
RT "Cloning of genes involved in carbazole degradation of Pseudomonas sp.
RT strain CA10: nucleotide sequences of genes and characterization of meta-
RT cleavage enzymes and hydrolase.";
RL J. Bacteriol. 179:4841-4849(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CA10;
RX PubMed=9244274; DOI=10.1128/jb.179.15.4850-4858.1997;
RA Sato S.I., Nam J.W., Kasuga K., Nojiri H., Yamane H., Omori T.;
RT "Identification and characterization of genes encoding carbazole 1,9a-
RT dioxygenase in Pseudomonas sp. strain CA10.";
RL J. Bacteriol. 179:4850-4858(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CA10;
RX PubMed=11371531; DOI=10.1128/jb.183.12.3663-3679.2001;
RA Nojiri H., Sekiguchi H., Maeda K., Urata M., Nakai S., Yoshida T., Habe H.,
RA Omori T.;
RT "Genetic characterization and evolutionary implications of a car gene
RT cluster in the carbazole degrader Pseudomonas sp. strain CA10.";
RL J. Bacteriol. 183:3663-3679(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pCAR1;
RX PubMed=12547188; DOI=10.1016/s0022-2836(02)01400-6;
RA Maeda K., Nojiri H., Shintani M., Yoshida T., Habe H., Omori T.;
RT "Complete nucleotide sequence of carbazole/dioxin-degrading plasmid pCAR1
RT in Pseudomonas resinovorans strain CA10 indicates its mosaicity and the
RT presence of large catabolic transposon Tn4676.";
RL J. Mol. Biol. 326:21-33(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CA10; PLASMID=pCAR1;
RX PubMed=15466034; DOI=10.1128/jb.186.20.6815-6823.2004;
RA Urata M., Miyakoshi M., Kai S., Maeda K., Habe H., Omori T., Yamane H.,
RA Nojiri H.;
RT "Transcriptional regulation of the ant operon, encoding two-component
RT anthranilate 1,2-dioxygenase, on the carbazole-degradative plasmid pCAR1 of
RT Pseudomonas resinovorans strain CA10.";
RL J. Bacteriol. 186:6815-6823(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pCAR1;
RX PubMed=16672459; DOI=10.1128/aem.72.5.3206-3216.2006;
RA Shintani M., Yano H., Habe H., Omori T., Yamane H., Tsuda M., Nojiri H.;
RT "Characterization of the replication, maintenance, and transfer features of
RT the IncP-7 plasmid pCAR1, which carries genes involved in carbazole and
RT dioxin degradation.";
RL Appl. Environ. Microbiol. 72:3206-3216(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pCAR1;
RX PubMed=17675379; DOI=10.1128/jb.00684-07;
RA Miyakoshi M., Shintani M., Terabayashi T., Kai S., Yamane H., Nojiri H.;
RT "Transcriptome analysis of Pseudomonas putida KT2440 harboring the
RT completely sequenced IncP-7 plasmid pCAR1.";
RL J. Bacteriol. 189:6849-6860(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pCAR1;
RX PubMed=19376894; DOI=10.1128/aem.02373-08;
RA Takahashi Y., Shintani M., Li L., Yamane H., Nojiri H.;
RT "Carbazole-degradative IncP-7 plasmid pCAR1.2 is structurally unstable in
RT Pseudomonas fluorescens Pf0-1, which accumulates catechol, the intermediate
RT of the carbazole degradation pathway.";
RL Appl. Environ. Microbiol. 75:3920-3929(2009).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pCAR1;
RX PubMed=19270415; DOI=10.1271/bbb.80665;
RA Takahashi Y., Shintani M., Yamane H., Nojiri H.;
RT "The complete nucleotide sequence of pCAR2: pCAR2 and pCAR1 were
RT structurally identical IncP-7 carbazole degradative plasmids.";
RL Biosci. Biotechnol. Biochem. 73:744-746(2009).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pCAR1;
RX PubMed=19134166; DOI=10.1186/1471-2164-10-12;
RA Miyakoshi M., Nishida H., Shintani M., Yamane H., Nojiri H.;
RT "High-resolution mapping of plasmid transcriptomes in different host
RT bacteria.";
RL BMC Genomics 10:12-12(2009).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pCAR1;
RX PubMed=19930443; DOI=10.1111/j.1462-2920.2009.02110.x;
RA Shintani M., Takahashi Y., Tokumaru H., Kadota K., Hara H., Miyakoshi M.,
RA Naito K., Yamane H., Nishida H., Nojiri H.;
RT "Response of the Pseudomonas host chromosomal transcriptome to carriage of
RT the IncP-7 plasmid pCAR1.";
RL Environ. Microbiol. 12:1413-1426(2010).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pCAR1;
RX PubMed=20639326; DOI=10.1128/jb.00591-10;
RA Yun C.S., Suzuki C., Naito K., Takeda T., Takahashi Y., Sai F.,
RA Terabayashi T., Miyakoshi M., Shintani M., Nishida H., Yamane H.,
RA Nojiri H.;
RT "Pmr, a histone-like protein H1 (H-NS) family protein encoded by the IncP-7
RT plasmid pCAR1, is a key global regulator that alters host function.";
RL J. Bacteriol. 192:4720-4731(2010).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND SUBUNIT.
RC STRAIN=CA10;
RX PubMed=12619671; DOI=10.1271/bbb.67.36;
RA Nojiri H., Taira H., Iwata K., Morii K., Nam J.W., Yoshida T., Habe H.,
RA Nakamura S., Shimizu K., Yamane H., Omori T.;
RT "Purification and characterization of meta-cleavage compound hydrolase from
RT a carbazole degrader Pseudomonas resinovorans strain CA10.";
RL Biosci. Biotechnol. Biochem. 67:36-45(2003).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-114, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=CA10;
RX PubMed=12651123; DOI=10.1016/s1046-5928(02)00676-9;
RA Riddle R.R., Gibbs P.R., Willson R.C., Benedik M.J.;
RT "Purification and properties of 2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-
RT dienoic acid hydrolase involved in microbial degradation of carbazole.";
RL Protein Expr. Purif. 28:182-189(2003).
CC -!- FUNCTION: Involved in the degradation of carbazole, a toxic N-
CC heterocyclic aromatic compound containing dibenzopyrrole system.
CC Catalyzes the hydrolytic cleavage of a carbon-carbon bond of 2-hydroxy-
CC 6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid (HOPDA) to yield
CC anthranilate. CarC is specific for 2-hydroxy-6-oxo-6-phenylhexa-2,4-
CC dienoic acid (6-phenyl-HODA), and has little activity toward 2-hydroxy-
CC 6-oxohepta-2,4-dienoic acid and 2-hydroxymuconic semialdehyde. The
CC effect of the presence of an amino group or hydroxyl group at the 2'-
CC position of phenyl moiety of 6-phenyl-HODA on the enzyme activity is
CC found to be small. {ECO:0000269|PubMed:12619671,
CC ECO:0000269|PubMed:12651123, ECO:0000269|PubMed:9244273}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,4E)-6-(2-aminophenyl)-2-hydroxy-6-oxohexa-2,4-dienoate +
CC H2O = (2E)-2-hydroxypenta-2,4-dienoate + anthranilate + H(+);
CC Xref=Rhea:RHEA:27870, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:60885, ChEBI:CHEBI:60886; EC=3.7.1.13;
CC Evidence={ECO:0000269|PubMed:12619671, ECO:0000269|PubMed:12651123};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.51 uM for 6-phenyl-HODA (at 50 mM sodium phosphate, pH 7.5, 25
CC degrees Celsius) {ECO:0000269|PubMed:12619671,
CC ECO:0000269|PubMed:12651123};
CC KM=4.6 uM for HOPDA (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:12619671, ECO:0000269|PubMed:12651123};
CC Vmax=3.3 mmol/min/mg enzyme with HOPDA as substrate (at pH 7.5 and 25
CC degrees Celsius) {ECO:0000269|PubMed:12619671,
CC ECO:0000269|PubMed:12651123};
CC Note=kcat is 2.14 sec(-1) for 6-phenyl-HODA (at 50 mM sodium
CC phosphate, pH 7.5, 25 degrees Celsius).;
CC pH dependence:
CC Optimum pH is between 7.0 and 7.5. {ECO:0000269|PubMed:12619671,
CC ECO:0000269|PubMed:12651123};
CC Temperature dependence:
CC Optimum temperature is 58 degrees Celsius.
CC {ECO:0000269|PubMed:12619671, ECO:0000269|PubMed:12651123};
CC -!- PATHWAY: Xenobiotic degradation; carbazole degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12619671,
CC ECO:0000269|PubMed:12651123}.
CC -!- SIMILARITY: Belongs to the DmpD/TodF/XylF esterase family.
CC {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; AB047548; BAB32769.1; -; Genomic_DNA.
DR EMBL; AB088420; BAC41548.1; -; Genomic_DNA.
DR RefSeq; NP_758570.1; NC_004444.1.
DR RefSeq; WP_011077881.1; NC_004444.1.
DR AlphaFoldDB; Q9AQM4; -.
DR SMR; Q9AQM4; -.
DR ESTHER; psest-bpdF; Carbon-carbon_bond_hydrolase.
DR BioCyc; MetaCyc:MON-15764; -.
DR BRENDA; 3.7.1.13; 7692.
DR UniPathway; UPA01031; -.
DR GO; GO:0102139; F:2-hydroxy-6-oxo-6-(2'-aminophenyl)-hexa-2,4dienoate hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0018768; F:2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoate hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IDA:UniProtKB.
DR GO; GO:0046232; P:carbazole catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Hydrolase; Plasmid.
FT CHAIN 1..290
FT /note="2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic
FT acid hydrolase"
FT /id="PRO_0000422736"
FT ACT_SITE 114
FT /evidence="ECO:0000305"
FT ACT_SITE 233
FT /evidence="ECO:0000250"
FT ACT_SITE 261
FT /evidence="ECO:0000250"
FT MUTAGEN 114
FT /note="S->A: 40-fold decrease in reduction in hydrolase
FT activity."
FT /evidence="ECO:0000269|PubMed:12651123"
SQ SEQUENCE 290 AA; 32252 MW; FF88FD90E69D365B CRC64;
MLNKAEQISE KSESAYVERF VNAGGVETRY LEAGKGQPVI LIHGGGAGAE SEGNWRNVIP
ILARHYRVIA MDMLGFGKTA KPDIEYTQDR RIRHLHDFIK AMNFDGKVSI VGNSMGGATG
LGVSVLHSEL VNALVLMGSA GLVVEIHEDL RPIINYDFTR EGMVHLVKAL TNDGFKIDDA
MINSRYTYAT DEATRKAYVA TMQWIREQGG LFYDPEFIRK VPVPTLVVHG KDDKVVPVET
AYKFLDLIDD SWGYIIPHCG HWAMIEHPED FANATLSFLS RRADITRAAA
