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Database: UniProt
Entry: A8TZ69_9PROT
LinkDB: A8TZ69_9PROT
Original site: A8TZ69_9PROT 
ID   A8TZ69_9PROT            Unreviewed;       203 AA.
AC   A8TZ69;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   13-SEP-2023, entry version 47.
DE   RecName: Full=2-hydroxychromene-2-carboxylate isomerase {ECO:0000256|PIRNR:PIRNR006386};
DE            EC=5.99.1.4 {ECO:0000256|PIRNR:PIRNR006386};
GN   ORFNames=BAL199_29225 {ECO:0000313|EMBL:EDP62351.1};
OS   alpha proteobacterium BAL199.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP62351.1, ECO:0000313|Proteomes:UP000003417};
RN   [1] {ECO:0000313|EMBL:EDP62351.1, ECO:0000313|Proteomes:UP000003417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL199 {ECO:0000313|EMBL:EDP62351.1,
RC   ECO:0000313|Proteomes:UP000003417};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-2007) 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:EDP62351.1}.
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DR   EMBL; ABHC01000021; EDP62351.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8TZ69; -.
DR   STRING; 331869.BAL199_29225; -.
DR   eggNOG; COG3917; Bacteria.
DR   OrthoDB; 5244108at2; -.
DR   Proteomes; UP000003417; 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   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR014440; HCCAis_GSTk.
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:UP000003417}.
FT   DOMAIN          6..193
FT                   /note="DSBA-like thioredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF01323"
FT   ACT_SITE        14
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006386-1"
SQ   SEQUENCE   203 AA;  23014 MW;  26C8FD4F784890E2 CRC64;
     MSKPVVRVYT DYKSPYAFIA VKPTYELAEA LDIELEWLPY TLRIAEYLGS VEERTEHSWR
     RVRYSYMDAR RYANKQGLVL KGPKRVYNGY YASAGMIFAQ RTGIFRAYHD TVFETFWKRE
     LDIDVLSEVS ALVASIGGDA AAFEGYAEGA GRAEQEAIVA EAEAMGVFGV PMFVFDGELF
     WGGDRIDLLR ERIEESRAAP ASE
//
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