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Database: UniProt/TrEMBL
Entry: T1X6N6_VARPD
LinkDB: T1X6N6_VARPD
Original site: T1X6N6_VARPD 
ID   T1X6N6_VARPD            Unreviewed;       197 AA.
AC   T1X6N6;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=2-hydroxychromene-2-carboxylate isomerase {ECO:0000256|PIRNR:PIRNR006386};
DE            EC=5.99.1.4 {ECO:0000256|PIRNR:PIRNR006386};
GN   ORFNames=VAPA_1c08790 {ECO:0000313|EMBL:AGU47999.1};
OS   Variovorax paradoxus B4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1246301 {ECO:0000313|EMBL:AGU47999.1, ECO:0000313|Proteomes:UP000016223};
RN   [1] {ECO:0000313|EMBL:AGU47999.1, ECO:0000313|Proteomes:UP000016223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:AGU47999.1,
RC   ECO:0000313|Proteomes:UP000016223};
RA   Schuldes J., Brandt U., Hiessl S., Wuebbeler J.H., Thuermer A.,
RA   Steinbuechel A., Daniel R.;
RT   "Genome sequence of Variovorax paradoxus B4.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003911; AGU47999.1; -; Genomic_DNA.
DR   RefSeq; WP_021005549.1; NC_022247.1.
DR   AlphaFoldDB; T1X6N6; -.
DR   KEGG; vpd:VAPA_1c08790; -.
DR   PATRIC; fig|1246301.3.peg.894; -.
DR   HOGENOM; CLU_069253_1_3_4; -.
DR   OrthoDB; 8560325at2; -.
DR   Proteomes; UP000016223; Chromosome 1.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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};
KW   Transferase {ECO:0000313|EMBL:AGU47999.1}.
FT   DOMAIN          4..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   197 AA;  21563 MW;  AC302F3E284DC9F0 CRC64;
     MTKTVEFYFD FGSPAAYLAA TQLPHVCADT GAELVWKPML LGGVFQATGN RSPAEVVPKG
     PYMTIDLKRF ARRYGVPFVH NPHFPINTLL LMRGATGLQM KEPARLGAYV DAVFHAMWVE
     PKNMNDPATV AAVLQNAGFD ATALLALAGT QEVKDRLRAV TQEAVARGVF GAPTMFVGDQ
     MFWGQDRLDF VREALDA
//
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