ID Q4FMF0_PELUB Unreviewed; 194 AA.
AC Q4FMF0;
DT 30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=2-hydroxychromene-2-carboxylate isomerase {ECO:0000256|PIRNR:PIRNR006386};
DE EC=5.99.1.4 {ECO:0000256|PIRNR:PIRNR006386};
GN Name=dsbA {ECO:0000313|EMBL:AAZ21639.1};
GN OrderedLocusNames=SAR11_0822 {ECO:0000313|EMBL:AAZ21639.1};
OS Pelagibacter ubique (strain HTCC1062).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae; Pelagibacter.
OX NCBI_TaxID=335992 {ECO:0000313|EMBL:AAZ21639.1, ECO:0000313|Proteomes:UP000002528};
RN [1] {ECO:0000313|EMBL:AAZ21639.1, ECO:0000313|Proteomes:UP000002528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC1062 {ECO:0000313|EMBL:AAZ21639.1,
RC ECO:0000313|Proteomes:UP000002528};
RX PubMed=16109880; DOI=10.1126/science.1114057;
RA Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA Carrington J.C., Mathur E.J.;
RT "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL Science 309:1242-1245(2005).
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; CP000084; AAZ21639.1; -; Genomic_DNA.
DR RefSeq; WP_011281972.1; NC_007205.1.
DR AlphaFoldDB; Q4FMF0; -.
DR STRING; 335992.SAR11_0822; -.
DR KEGG; pub:SAR11_0822; -.
DR eggNOG; COG3917; Bacteria.
DR HOGENOM; CLU_069253_1_3_5; -.
DR OrthoDB; 5244108at2; -.
DR Proteomes; UP000002528; Chromosome.
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:AAZ21639.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002528}.
FT DOMAIN 4..190
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 194 AA; 22783 MW; 7A089FC6D58CC5EE CRC64;
MIKEIDFYFD FISPYAYLAY QKIQTLPKDI RINYKPILLG GLHNLEGITA PAFIKPKLKH
MINDCLLIAK KNNFDFKWNS KFPLNSLIIM RGYLDISSSN QAQYIKTMFD AYWKDDLDIS
KEEILIPLLE QCKIDKDIFF KTIKDPVIKE KLKNATKNAH EKEVFGAPTF IVNNKIFWGQ
DRLEFALDEY NKVD
//
