ID   PHDI_NOCSK              Reviewed;         387 AA.
AC   O24721; Q9FBF3;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 2.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=1-hydroxy-2-naphthoate 1,2-dioxygenasee;
DE            EC=1.13.11.38;
DE   AltName: Full=1-hydroxy-2-naphthoate-degrading enzyme;
DE   AltName: Full=1-hydroxy-2-naphthoic acid dioxygenase;
GN   Name=phdI;
OS   Nocardioides sp. (strain KP7).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=102632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KP7;
RX   PubMed=9335300; DOI=10.1128/jb.179.20.6488-6494.1997;
RA   Iwabuchi T., Harayama S.;
RT   "Biochemical and genetic characterization of 2-carboxybenzaldehyde
RT   dehydrogenase, an enzyme involved in phenanthrene degradation by
RT   Nocardioides sp. strain KP7.";
RL   J. Bacteriol. 179:6488-6494(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-56, FUNCTION,
RP   COFACTOR, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=KP7;
RX   PubMed=9525941; DOI=10.1074/jbc.273.14.8332;
RA   Iwabuchi T., Harayama S.;
RT   "Biochemical and molecular characterization of 1-hydroxy-2-naphthoate
RT   dioxygenase from Nocardioides sp. KP7.";
RL   J. Biol. Chem. 273:8332-8336(1998).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA   Shearer A.G., Altman T., Rhee C.D.;
RT   "Finding sequences for over 270 orphan enzymes.";
RL   PLoS ONE 9:E97250-E97250(2014).
CC   -!- FUNCTION: Dioxygenase involved in phenanthrene catabolism by mediating
CC       cleavage of 1-hydroxy-2-naphthoate. {ECO:0000269|PubMed:9525941}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hydroxy-2-naphthoate + O2 = (3Z)-4-(2-carboxyphenyl)-2-
CC         oxobut-3-enoate + H(+); Xref=Rhea:RHEA:14749, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:15992, ChEBI:CHEBI:58794;
CC         EC=1.13.11.38; Evidence={ECO:0000269|PubMed:9525941};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:9525941};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=10 uM for 1-hydroxy-2-naphthoate {ECO:0000269|PubMed:9525941};
CC         Note=kcat is 114 sec(-1) for 1-hydroxy-2-naphthoate.;
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:9525941};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:9525941}.
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DR   EMBL; D89987; BAA31235.2; -; Genomic_DNA.
DR   EMBL; AB000735; BAA23262.1; -; Genomic_DNA.
DR   AlphaFoldDB; O24721; -.
DR   SMR; O24721; -.
DR   BRENDA; 1.13.11.38; 4363.
DR   GO; GO:0018582; F:1-hydroxy-2-naphthoate 1,2-dioxygenase activity; IDA:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR   GO; GO:0042216; P:phenanthrene catabolic process; IDA:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR013096; Cupin_2.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF07883; Cupin_2; 2.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; Direct protein sequencing; Iron; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9525941"
FT   CHAIN           2..387
FT                   /note="1-hydroxy-2-naphthoate 1,2-dioxygenasee"
FT                   /id="PRO_0000430446"
FT   CONFLICT        12
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        54
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="A -> G (in Ref. 2; BAA23262)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350
FT                   /note="L -> F (in Ref. 2; BAA23262)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        378
FT                   /note="P -> A (in Ref. 2; BAA23262)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   387 AA;  43082 MW;  6E4EB87B8413A4DE CRC64;
     MNSSNTGAPE AAQAATLEAF DRRAAEQYLR GQWIAEEHLM RAIGGPRPAG IPYRWEWKSV
     EVALDEATIA LGPVDTARRH LTFVNPGLMD RGSATTHTIS AGFQLVKPGE VCWSHRHTMS
     AVRFVTKGHP DAFTAVDGER LPMEDFDLLI TPRFSWHDHH NSGDADVVWL DGLDIGLLQS
     LGAVFYEPYG DDSQNVRPSS SEGIGTRSHW LRPTWERGRE SRLPIRYPWK EVNARLDVYD
     LDAGTPYDGL ALRYANPVTG GPTMATMDCW VQRLAPGFDG KSHRRSSSAI TYVISGSGTM
     VTEDETITFN RGDVISLPNW TNFRWTNDSE IEPVLLFSMH DIPALEAFGL LYEEPEAILN
     ATPAPINPTP SLNPIYRPGA FYDQDEL