ID K0CA16_CYCSP Unreviewed; 198 AA.
AC K0CA16;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=2-hydroxychromene-2-carboxylate isomerase {ECO:0000256|PIRNR:PIRNR006386};
DE EC=5.99.1.4 {ECO:0000256|PIRNR:PIRNR006386};
GN Name=dsbA2 {ECO:0000313|EMBL:AFT68251.1};
GN OrderedLocusNames=Q91_2218 {ECO:0000313|EMBL:AFT68251.1};
OS Cycloclasticus sp. (strain P1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Cycloclasticus.
OX NCBI_TaxID=385025 {ECO:0000313|EMBL:AFT68251.1, ECO:0000313|Proteomes:UP000006282};
RN [1] {ECO:0000313|EMBL:AFT68251.1, ECO:0000313|Proteomes:UP000006282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1 {ECO:0000313|EMBL:AFT68251.1,
RC ECO:0000313|Proteomes:UP000006282};
RX PubMed=23144416; DOI=10.1128/JB.01837-12;
RA Lai Q., Li W., Wang B., Yu Z., Shao Z.;
RT "Complete genome sequence of the pyrene-degrading bacterium Cycloclasticus
RT sp. strain P1.";
RL J. Bacteriol. 194:6677-6677(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; CP003230; AFT68251.1; -; Genomic_DNA.
DR RefSeq; WP_015007020.1; NC_018697.1.
DR AlphaFoldDB; K0CA16; -.
DR STRING; 385025.Q91_2218; -.
DR KEGG; cyq:Q91_2218; -.
DR PATRIC; fig|385025.3.peg.2265; -.
DR HOGENOM; CLU_069253_1_3_6; -.
DR Proteomes; UP000006282; 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, ECO:0000313|EMBL:AFT68251.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006282}.
FT DOMAIN 5..194
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 198 AA; 22745 MW; 1191A440DFAB2C7C CRC64;
MQESIDFYFD MMSPFSYLAH TQLPDLARKY GLTVKYLPMS IPVAKIAAGN YGPSNREVPA
KIKVMLQDIK RWAAHYDVPF TFPKNLEIEP WNIGVLYAND KDQAEAYVNA AYAKIWADGC
DPTDMAELSQ VADQLGWNAD EFIAYVQSNE GQTRFRKACV EAHKEGVFGA PIMMLDDQAW
WGNDRFMFME EYLKDRKN
//
