NSAC_SPHXE
ID NSAC_SPHXE Reviewed; 298 AA.
AC P74836;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=1,2-dihydroxynaphthalene dioxygenase;
DE Short=1,2-DHN dioxygenase;
DE Short=DHNDO;
DE EC=1.13.11.56;
GN Name=nsaC;
OS Sphingobium xenophagum.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=121428;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=DSM 6383 / KCTC 2978 / NBRC 107872 / BN6;
RX PubMed=16804169; DOI=10.1099/mic.0.28783-0;
RA Keck A., Conradt D., Mahler A., Stolz A., Mattes R., Klein J.;
RT "Identification and functional analysis of the genes for
RT naphthalenesulfonate catabolism by Sphingomonas xenophaga BN6.";
RL Microbiology 152:1929-1940(2006).
RN [2]
RP PROTEIN SEQUENCE OF 2-30, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, INDUCTION, AND SUBUNIT.
RX PubMed=2050635; DOI=10.1128/jb.173.12.3795-3802.1991;
RA Kuhm A.E., Stolz A., Ngai K.L., Knackmuss H.J.;
RT "Purification and characterization of a 1,2-dihydroxynaphthalene
RT dioxygenase from a bacterium that degrades naphthalenesulfonic acids.";
RL J. Bacteriol. 173:3795-3802(1991).
CC -!- FUNCTION: Involved in the naphthalene and naphthalenesulfonate
CC catabolic pathway. Catalyzes the meta-cleavage of 1,2-
CC dihydroxynaphthalene (1,2-DHN) to yield 2-hydroxychromene-2-carboxylic
CC acid. Can also cleave 1,2,5-trihydroxynaphthalene (1,2,5-THN), 1,2,6-
CC trihydroxynaphthalene (1,2,6-THN), 1,2,7-trihydroxynaphthalene (1,2,7-
CC THN), 2,3-dihydroxybiphenyl, 3,4-dihydroxybiphenyl, catechol, 3-
CC methylcatechol and 4-methylcatechol. {ECO:0000269|PubMed:16804169,
CC ECO:0000269|PubMed:2050635}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=naphthalene-1,2-diol + O2 = 2-hydroxychromene-2-carboxylate +
CC H(+); Xref=Rhea:RHEA:27310, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17435, ChEBI:CHEBI:59350; EC=1.13.11.56;
CC Evidence={ECO:0000269|PubMed:2050635};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:2050635};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=34 uM for 1,2-DHN (at pH 5.5) {ECO:0000269|PubMed:2050635};
CC Note=Under alkaline conditions (pH 11), the cleavage of 1,2-DHN yield
CC cis-2'-hydroxybenzalpyruvate.;
CC -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:2050635}.
CC -!- INDUCTION: By naphthalene-2-sulfonic acid.
CC {ECO:0000269|PubMed:2050635}.
CC -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; U65001; AAB06725.2; -; Genomic_DNA.
DR AlphaFoldDB; P74836; -.
DR SMR; P74836; -.
DR KEGG; ag:AAB06725; -.
DR BRENDA; 1.13.11.56; 10830.
DR SABIO-RK; P74836; -.
DR UniPathway; UPA00082; -.
DR GO; GO:0018554; F:1,2-dihydroxynaphthalene dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IDA:UniProtKB.
DR GO; GO:1901170; P:naphthalene catabolic process; IMP:UniProtKB.
DR GO; GO:0042178; P:xenobiotic catabolic process; IEA:InterPro.
DR Gene3D; 3.10.180.10; -; 2.
DR InterPro; IPR017626; DiOHbiphenyl_dOase.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR037523; VOC.
DR InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2.
DR Pfam; PF00903; Glyoxalase; 1.
DR SUPFAM; SSF54593; SSF54593; 1.
DR TIGRFAMs; TIGR03213; 23dbph12diox; 1.
DR PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
DR PROSITE; PS51819; VOC; 2.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing;
KW Iron; Metal-binding; Oxidoreductase; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2050635"
FT CHAIN 2..298
FT /note="1,2-dihydroxynaphthalene dioxygenase"
FT /id="PRO_0000423055"
FT DOMAIN 6..121
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 146..267
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 149
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 196..197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 298 AA; 33301 MW; EF7DC9622C5F89AD CRC64;
MSSVSELGYL GMSVTDLDAW RAYAAEVAGM EVVDEGESDR IYLRMDLWHH RIALIKGDTD
DLAYMGWRLG DPTEFESMVE KLTNAGIAVT VASDAEARER RVLGLAKLTD PGGNPTEIFY
GPQVDAHKPF HPGRPMFGKF VTGSEGIGHC ILRQDDVEAA AAFYRLLGLR GSVEYQLHLP
NGMVAMPYFM HCNERQHSVA FGLGPMEKRI NHLMFEYTEL DDLGLAHDIV RERQIDVALQ
LGKHANDLAL TFYCANPSGW LWEFGWGARK APAQQEFYTR DIFGHGNEAQ GYGMDVPL
