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Database: UniProt
Entry: I3V373_PSEPU
LinkDB: I3V373_PSEPU
Original site: I3V373_PSEPU 
ID   I3V373_PSEPU            Unreviewed;       204 AA.
AC   I3V373;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=2-hydroxychromene-2-carboxylate isomerase {ECO:0000256|PIRNR:PIRNR006386};
DE            EC=5.99.1.4 {ECO:0000256|PIRNR:PIRNR006386};
GN   ORFNames=YSA_09988 {ECO:0000313|EMBL:AFK72194.1};
OS   Pseudomonas putida ND6.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=231023 {ECO:0000313|EMBL:AFK72194.1, ECO:0000313|Proteomes:UP000005268};
RN   [1] {ECO:0000313|EMBL:AFK72194.1, ECO:0000313|Proteomes:UP000005268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND6 {ECO:0000313|EMBL:AFK72194.1,
RC   ECO:0000313|Proteomes:UP000005268};
RX   PubMed=22933774; DOI=10.1128/JB.01190-12;
RA   Li S., Zhao H., Li Y., Niu S., Cai B.;
RT   "Complete Genome Sequence of the Naphthalene-Degrading Pseudomonas putida
RT   Strain ND6.";
RL   J. Bacteriol. 194:5154-5155(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxychromene-2-carboxylate = (3E)-4-(2-hydroxyphenyl)-2-
CC         oxobut-3-enoate; Xref=Rhea:RHEA:27401, ChEBI:CHEBI:59350,
CC         ChEBI:CHEBI:59353; EC=5.99.1.4;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006386};
CC   -!- SIMILARITY: Belongs to the GST superfamily. NadH family.
CC       {ECO:0000256|PIRNR:PIRNR006386}.
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DR   EMBL; CP003588; AFK72194.1; -; Genomic_DNA.
DR   RefSeq; WP_014756430.1; NC_017986.1.
DR   AlphaFoldDB; I3V373; -.
DR   KEGG; ppi:YSA_09988; -.
DR   PATRIC; fig|231023.4.peg.4804; -.
DR   HOGENOM; CLU_069253_1_3_6; -.
DR   Proteomes; UP000005268; Chromosome.
DR   GO; GO:0018845; F:2-hydroxychromene-2-carboxylate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:1901170; P:naphthalene catabolic process; IEA:InterPro.
DR   CDD; cd03022; DsbA_HCCA_Iso; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR014440; HCCAis_GSTk.
DR   InterPro; IPR044087; NahD-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR42943; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR   PANTHER; PTHR42943:SF2; GLUTATHIONE S-TRANSFERASE KAPPA 1; 1.
DR   Pfam; PF01323; DSBA; 1.
DR   PIRSF; PIRSF006386; HCCAis_GSTk; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PIRNR:PIRNR006386}.
FT   DOMAIN          5..195
FT                   /note="DSBA-like thioredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF01323"
FT   ACT_SITE        13
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006386-1"
SQ   SEQUENCE   204 AA;  22023 MW;  23250620E59FB49A CRC64;
     MHTSVDFFFD LGSPASYLAW TQLPNLCARH GATLRYRPML LGGVFQATGN ASPAMIPAKG
     RYMFTDLARF AERYGVPLGM PPGFPVNTLT LMRGVTGTQL HSPDRFEALL SVLFTGLWVQ
     RRNLSDSAVL NEALVQAGFD PQVFHALAAD SEVKAALKQA TEAAVARGVF GAPTCFVGDG
     MFFGQDRLDF VEEALRQGAS SLSS
//
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