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Database: UniProt
Entry: A0A0C4YPJ2_9BURK
LinkDB: A0A0C4YPJ2_9BURK
Original site: A0A0C4YPJ2_9BURK 
ID   A0A0C4YPJ2_9BURK        Unreviewed;       200 AA.
AC   A0A0C4YPJ2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=2-hydroxychromene-2-carboxylate isomerase {ECO:0000256|PIRNR:PIRNR006386};
DE            EC=5.99.1.4 {ECO:0000256|PIRNR:PIRNR006386};
GN   ORFNames=RR42_s0911 {ECO:0000313|EMBL:AJG22501.1};
OS   Cupriavidus basilensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG22501.1, ECO:0000313|Proteomes:UP000031843};
RN   [1] {ECO:0000313|EMBL:AJG22501.1, ECO:0000313|Proteomes:UP000031843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4G11 {ECO:0000313|EMBL:AJG22501.1};
RX   PubMed=25977418;
RA   Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA   Chakraborty R., Arkin A.P., Deutschbauer A.;
RT   "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT   Oak Ridge Field Research Center Site.";
RL   Genome Announc. 3:0-0(2015).
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; CP010537; AJG22501.1; -; Genomic_DNA.
DR   RefSeq; WP_043354006.1; NZ_CP010537.1.
DR   AlphaFoldDB; A0A0C4YPJ2; -.
DR   STRING; 68895.RR42_s0911; -.
DR   KEGG; cbw:RR42_s0911; -.
DR   OrthoDB; 8560325at2; -.
DR   Proteomes; UP000031843; Chromosome secondary.
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, ECO:0000313|EMBL:AJG22501.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031843}.
FT   DOMAIN          6..196
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   200 AA;  21945 MW;  98B915F5B2F74448 CRC64;
     MSRTAEFYFD VGSPASYLAW TQLPTICEET GGTLVYKPIL LGGVFQATGN ASPATIPAKG
     AYTNIDSARH ARLYGVPYQS NPHFPVISLT LMRAATGVQM RMPERFQDYL RSVLHALWVD
     ALNLNEPQVV AKTLVDAGFD IEAILALAND AEVKSQLRST TEEAVKRGVF GAPTIFVGEH
     MFFGQDRLEW VCHALQGKPL
//
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