ID A0A0F4JAF9_9ACTN Unreviewed; 249 AA.
AC A0A0F4JAF9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=2-hydroxychromene-2-carboxylate isomerase {ECO:0000256|PIRNR:PIRNR006386};
DE EC=5.99.1.4 {ECO:0000256|PIRNR:PIRNR006386};
GN ORFNames=VR44_18635 {ECO:0000313|EMBL:KJY31180.1};
OS Streptomyces katrae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY31180.1, ECO:0000313|Proteomes:UP000033551};
RN [1] {ECO:0000313|EMBL:KJY31180.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY31180.1};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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:KJY31180.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JZWV01000511; KJY31180.1; -; Genomic_DNA.
DR RefSeq; WP_045948663.1; NZ_JZWV01000511.1.
DR AlphaFoldDB; A0A0F4JAF9; -.
DR PATRIC; fig|68223.7.peg.8336; -.
DR OrthoDB; 5244108at2; -.
DR Proteomes; UP000033551; 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, ECO:0000313|EMBL:KJY31180.1}.
FT DOMAIN 18..209
FT /note="DSBA-like thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF01323"
FT REGION 219..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 24
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006386-1"
SQ SEQUENCE 249 AA; 27746 MW; 0CF7AFE9FFE6D040 CRC64;
MSEAAPSPGA RRQAPPRFYF SLRSPYSWLA HQELLARHPD VVERLEWRPF WEPDEESARA
LEAAGGRFPY VAMSREKHLY ILQDVRRLTR ERGLEPTWPV DREPCWEVPH LAWLVAQDAG
RGPEFVGRVY RARWQEGRDI CDPSVIGELG AELGLPAERL AGAARDPELR ARGVSALLDV
WRDGVFGVPF LIDGHDKFWG TDRISDFARS VRGRATRDGN RKCAKAGSPN APADTVARSA
DGGHAGGCG
//
