ID Q07H84_RHOP5 Unreviewed; 207 AA.
AC Q07H84;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=2-hydroxychromene-2-carboxylate isomerase {ECO:0000256|PIRNR:PIRNR006386};
DE EC=5.99.1.4 {ECO:0000256|PIRNR:PIRNR006386};
GN OrderedLocusNames=RPE_4781 {ECO:0000313|EMBL:ABJ08700.1};
OS Rhodopseudomonas palustris (strain BisA53).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316055 {ECO:0000313|EMBL:ABJ08700.1};
RN [1] {ECO:0000313|EMBL:ABJ08700.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisA53 {ECO:0000313|EMBL:ABJ08700.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL Submitted (SEP-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}.
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DR EMBL; CP000463; ABJ08700.1; -; Genomic_DNA.
DR AlphaFoldDB; Q07H84; -.
DR STRING; 316055.RPE_4781; -.
DR KEGG; rpe:RPE_4781; -.
DR eggNOG; COG3917; Bacteria.
DR HOGENOM; CLU_069253_1_3_5; -.
DR OrthoDB; 5244108at2; -.
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:SF13; GLUTATHIONE S-TRANSFERASE KAPPA-RELATED; 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}.
FT DOMAIN 5..197
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 207 AA; 23372 MW; 61D2D7CCE26DBCB0 CRC64;
MSQPIDYYFS LQSPWAYIGH EIFRELVSAY DLKVNYKPVV LIELFEETGG MPLGKRHPVR
QHYRLVELQR WRAKRGLDFH LQPKHWPFNA KLADSVVIAA VESGLDPDSY LRQAYPAMWE
RQLDLADPQV LVTLADAAGL PGTSLVERAA SAGIGEIYQQ NRQHALDAGV FGSPAYVLNG
EVFWGQDRLD LLDDALKSGR PPFRPPS
//
