ID B6B9P7_9RHOB Unreviewed; 200 AA.
AC B6B9P7;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, 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=RBY4I_470 {ECO:0000313|EMBL:EDZ45263.1};
OS Rhodobacterales bacterium Y4I.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX NCBI_TaxID=439496 {ECO:0000313|EMBL:EDZ45263.1, ECO:0000313|Proteomes:UP000005133};
RN [1] {ECO:0000313|EMBL:EDZ45263.1, ECO:0000313|Proteomes:UP000005133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y4I {ECO:0000313|EMBL:EDZ45263.1,
RC ECO:0000313|Proteomes:UP000005133};
RA Moran M.A., Buchan A., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) 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; DS995281; EDZ45263.1; -; Genomic_DNA.
DR AlphaFoldDB; B6B9P7; -.
DR STRING; 439496.RBY4I_470; -.
DR eggNOG; COG3917; Bacteria.
DR HOGENOM; CLU_069253_1_3_5; -.
DR OrthoDB; 5244108at2; -.
DR Proteomes; UP000005133; 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:UP000005133}.
FT DOMAIN 4..195
FT /note="DSBA-like thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF01323"
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006386-1"
SQ SEQUENCE 200 AA; 21243 MW; 8EF09A1CA2626552 CRC64;
MAAIDFYFST LSPFAYLAGT RPWQIAARHG AEVTCKPLDI LALFARTGGT PPGERHPARQ
EYRLIELQRQ ADKLGLPINL KPAHWPANAA PSSYAIIAAQ NAGGGDMGEL VHSILRACWA
EEKDIADDAV IRACLAGAGF DPALADSGLL AGAETYAQNL EDAVTAGVFG APFWVTADGA
RFWGQDRLED LDAHLAEAAA
//