ID A0A248JNS2_9PROT Unreviewed; 201 AA.
AC A0A248JNS2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=2-hydroxychromene-2-carboxylate isomerase {ECO:0000256|PIRNR:PIRNR006386};
DE EC=5.99.1.4 {ECO:0000256|PIRNR:PIRNR006386};
GN ORFNames=Y958_04345 {ECO:0000313|EMBL:ASG20140.1};
OS Nitrospirillum amazonense CBAmc.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Nitrospirillum.
OX NCBI_TaxID=1441467 {ECO:0000313|EMBL:ASG20140.1, ECO:0000313|Proteomes:UP000197153};
RN [1] {ECO:0000313|EMBL:ASG20140.1, ECO:0000313|Proteomes:UP000197153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBAmC {ECO:0000313|EMBL:ASG20140.1,
RC ECO:0000313|Proteomes:UP000197153};
RA Schwab S., dos Santos Teixeira K.R., Simoes Araujo J.L., Soares Vidal M.,
RA Borges de Freitas H.R., Rivello Crivelaro A.L., Bueno de Camargo Nunes A.,
RA dos Santos C.M., Palmeira da Silva Rosa D., da Silva Padilha D.,
RA da Silva E., Araujo Terra L., Soares Mendes V., Farinelli L.,
RA Magalhaes Cruz L., Baldani J.I.;
RT "Complete genome sequence of Nitrospirillum amazonense strain CBAmC, an
RT endophytic nitrogen-fixing and plant growth-promoting bacterium, isolated
RT from sugarcane.";
RL Submitted (JUN-2017) 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; CP022110; ASG20140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248JNS2; -.
DR KEGG; nao:Y958_04345; -.
DR Proteomes; UP000197153; Chromosome 1.
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, ECO:0000313|EMBL:ASG20140.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000197153}.
FT DOMAIN 6..194
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 201 AA; 22002 MW; 45634C4733C62BF8 CRC64;
MAAQPLDFYF DFASPYGYFA AMAIDELAAR HGRTVAWHPI LLGAVFKSTG VTATVLRPLQ
GDYLRHDVMR SARYYGLPLV WPQVMPINAV ASSRAYYWTA ARDIGLARSL AKALYRAHWQ
EGRDISGVDV VADVATGIGM DADSLKAGMQ EPAVKDALRV ATDAAMARGV FGSPFIFVDG
EGFWGADRLV QVERWLAQGG W
//
