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Database: UniProt
Entry: A0A1L3JAG7_9SPHN
LinkDB: A0A1L3JAG7_9SPHN
Original site: A0A1L3JAG7_9SPHN 
ID   A0A1L3JAG7_9SPHN        Unreviewed;       202 AA.
AC   A0A1L3JAG7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=2-hydroxychromene-2-carboxylate isomerase {ECO:0000256|PIRNR:PIRNR006386};
DE            EC=5.99.1.4 {ECO:0000256|PIRNR:PIRNR006386};
GN   ORFNames=LPB140_04145 {ECO:0000313|EMBL:APG62130.1};
OS   Sphingorhabdus lutea.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingorhabdus.
OX   NCBI_TaxID=1913578 {ECO:0000313|EMBL:APG62130.1, ECO:0000313|Proteomes:UP000242561};
RN   [1] {ECO:0000313|EMBL:APG62130.1, ECO:0000313|Proteomes:UP000242561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0140 {ECO:0000313|EMBL:APG62130.1,
RC   ECO:0000313|Proteomes:UP000242561};
RA   Kim E., Yi H.;
RT   "Sphingorhabdus sp. LPB0140, isolated from marine environment.";
RL   Submitted (NOV-2016) 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; CP018154; APG62130.1; -; Genomic_DNA.
DR   RefSeq; WP_072558780.1; NZ_CP018154.1.
DR   AlphaFoldDB; A0A1L3JAG7; -.
DR   STRING; 1913578.LPB140_04145; -.
DR   KEGG; sphl:LPB140_04145; -.
DR   OrthoDB; 5244108at2; -.
DR   Proteomes; UP000242561; 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:APG62130.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242561}.
FT   DOMAIN          5..200
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   202 AA;  22871 MW;  C9224D19715DEE23 CRC64;
     MSKRIEFFFD LSSPWTCLAF HNIRPIIQEN DAQIIWRPIL VGGIFNAVNK SVYAMREDLG
     GPKMRHYMKS LKDWSKWSGV EMNFPSAHHP LKSVLAMRVC CALEDNQPAL EKFMEIAFAD
     HFAHQVNLDD AEILAQSIAK AGFDAQDILQ QTQSQEVKDR LRHNGEELIS RGGYGSPSIF
     VDGDDMYFGN DQLPLIAAKL KA
//
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