ID A3WX54_9BRAD Unreviewed; 201 AA.
AC A3WX54;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 08-NOV-2023, entry version 56.
DE RecName: Full=2-hydroxychromene-2-carboxylate isomerase {ECO:0000256|PIRNR:PIRNR006386};
DE EC=5.99.1.4 {ECO:0000256|PIRNR:PIRNR006386};
GN ORFNames=NB311A_18256 {ECO:0000313|EMBL:EAQ35434.1};
OS Nitrobacter sp. Nb-311A.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Nitrobacter.
OX NCBI_TaxID=314253 {ECO:0000313|EMBL:EAQ35434.1, ECO:0000313|Proteomes:UP000003725};
RN [1] {ECO:0000313|EMBL:EAQ35434.1, ECO:0000313|Proteomes:UP000003725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nb-311A {ECO:0000313|EMBL:EAQ35434.1,
RC ECO:0000313|Proteomes:UP000003725};
RA Waterbury J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (JAN-2006) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAQ35434.1}.
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DR EMBL; AAMY01000011; EAQ35434.1; -; Genomic_DNA.
DR RefSeq; WP_009799967.1; NZ_CH672421.1.
DR AlphaFoldDB; A3WX54; -.
DR STRING; 314253.NB311A_18256; -.
DR HOGENOM; CLU_069253_1_3_5; -.
DR OrthoDB; 5244108at2; -.
DR Proteomes; UP000003725; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000003725}.
FT DOMAIN 2..196
FT /note="DSBA-like thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF01323"
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006386-1"
SQ SEQUENCE 201 AA; 22579 MW; 7CA1129661D7155A CRC64;
MIEFFFDCSS PWTYLAFHNI QPMAKEFGEQ ISWRPVSVGG IFNAINPSVY ASRENPVAAK
VHYMRKDLAD WARSAGLAIK MPPTVFPVNS IKAMRGCLWL GNDAMVPFAR AVFEAYWRDD
KDISREPVLG EICRSLDIDP EKLLTGIGDE GIKNELKANT DEAIARGAFG SPTIFLDKTD
MYFGNDRLPL IREALQRKKA A
//