ID A0A0Q9F7Q2_9GAMM Unreviewed; 211 AA.
AC A0A0Q9F7Q2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=2-hydroxychromene-2-carboxylate isomerase {ECO:0000256|PIRNR:PIRNR006386};
DE EC=5.99.1.4 {ECO:0000256|PIRNR:PIRNR006386};
GN ORFNames=ASE45_04325 {ECO:0000313|EMBL:KRD71075.1};
OS Lysobacter sp. Root96.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1736612 {ECO:0000313|EMBL:KRD71075.1, ECO:0000313|Proteomes:UP000050805};
RN [1] {ECO:0000313|EMBL:KRD71075.1, ECO:0000313|Proteomes:UP000050805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root96 {ECO:0000313|EMBL:KRD71075.1,
RC ECO:0000313|Proteomes:UP000050805};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRD71075.1, ECO:0000313|Proteomes:UP000050805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root96 {ECO:0000313|EMBL:KRD71075.1,
RC ECO:0000313|Proteomes:UP000050805};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRD71075.1}.
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DR EMBL; LMJN01000001; KRD71075.1; -; Genomic_DNA.
DR RefSeq; WP_055903587.1; NZ_LMJN01000001.1.
DR AlphaFoldDB; A0A0Q9F7Q2; -.
DR STRING; 1736612.ASE45_04325; -.
DR OrthoDB; 5244108at2; -.
DR Proteomes; UP000050805; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050805}.
FT DOMAIN 5..196
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 211 AA; 22899 MW; 08171807AAAD8319 CRC64;
MAARVDYYFS LISPYAYFGH AAFLDAVREA GAEVAYRPSR IFDLFAANGG LPLGQRAPAR
QRYRLIELQR WRAKRGLPLN LAPRYFPLDP GLADRCAIAL VAAGADPAAY MDAAFRALWV
HDADIAAPAV LAELLTRHGF DAAPVLAAAD AAETVAAYQR NTEAAIAADL PGLPGYVLDG
EPFWGQDRVE DLREALISGR APFRIGQDDR A
//
