FLNB_TERSD
ID FLNB_TERSD Reviewed; 357 AA.
AC Q93UV4;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Fluoren-9-ol dehydrogenase {ECO:0000303|PubMed:15317800};
DE EC=1.1.1.256 {ECO:0000269|PubMed:15317800};
DE AltName: Full=1,1a-dihydroxy-1-hydro-9-fluorenone dehydrogenase {ECO:0000303|PubMed:15317800};
DE Short=DHF dehydrogenase {ECO:0000303|PubMed:15317800};
GN Name=flnB {ECO:0000303|PubMed:15317800};
GN Synonyms=ORF4 {ECO:0000303|PubMed:11322788, ECO:0000303|Ref.1};
OS Terrabacter sp. (strain DBF63).
OG Plasmid pDBF1 {ECO:0000312|EMBL:BAE45091.1}.
OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; Terrabacter;
OC unclassified Terrabacter.
OX NCBI_TaxID=150395 {ECO:0000312|EMBL:BAB55885.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DBF63; PLASMID=pDBF1;
RX DOI=10.1016/S0922-338X(97)81997-6;
RA Kasuga K., Nojiri H., Yamane H., Kodama T., Omori T.;
RT "Cloning and characterization of genes involved in the degradation of
RT dibenzofuran by Terrabacter sp. strain DBF63.";
RL J. Ferment. Bioeng. 84:387-399(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DBF63; PLASMID=pDBF1;
RX PubMed=11322788; DOI=10.1006/bbrc.2001.4763;
RA Kasuga K., Habe H., Chung J., Yoshida T., Nojiri H., Yamane H., Omori T.;
RT "Isolation and characterization of the genes encoding a novel oxygenase
RT component of angular dioxygenase from the gram-positive dibenzofuran-
RT degrader Terrabacter sp. strain DBF63.";
RL Biochem. Biophys. Res. Commun. 283:195-204(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=DBF63; PLASMID=pDBF1;
RX PubMed=15317800; DOI=10.1128/jb.186.17.5938-5944.2004;
RA Habe H., Chung J., Kato H., Ayabe Y., Kasuga K., Yoshida T., Nojiri H.,
RA Yamane H., Omori T.;
RT "Characterization of the upper pathway genes for fluorene metabolism in
RT Terrabacter sp. strain DBF63.";
RL J. Bacteriol. 186:5938-5944(2004).
CC -!- FUNCTION: Catalyzes the dehydrogenation of both 9-fluorenol and 1,1a-
CC dihydroxy-1-hydro-9-fluorenone to produce 9-fluorenone and 2'-carboxy-
CC 2,3- dihydroxybiphenyl, respectively. {ECO:0000269|PubMed:15317800}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9H-fluoren-9-ol + NADP(+) = 9H-fluoren-9-one + H(+) + NADPH;
CC Xref=Rhea:RHEA:12212, ChEBI:CHEBI:15378, ChEBI:CHEBI:16904,
CC ChEBI:CHEBI:17922, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.256; Evidence={ECO:0000269|PubMed:15317800};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9H-fluoren-9-ol + NAD(+) = 9H-fluoren-9-one + H(+) + NADH;
CC Xref=Rhea:RHEA:12216, ChEBI:CHEBI:15378, ChEBI:CHEBI:16904,
CC ChEBI:CHEBI:17922, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.256; Evidence={ECO:0000269|PubMed:15317800};
CC -!- PATHWAY: Aromatic compound metabolism. {ECO:0000305|PubMed:15317800}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000255|RuleBase:RU000363}.
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DR EMBL; AP008980; BAE45091.1; -; Genomic_DNA.
DR EMBL; AB054975; BAB55885.1; -; Genomic_DNA.
DR EMBL; AB095015; BAC75992.1; -; Genomic_DNA.
DR AlphaFoldDB; Q93UV4; -.
DR SMR; Q93UV4; -.
DR KEGG; ag:BAC75992; -.
DR GO; GO:0018461; F:fluoren-9-ol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0019429; P:fluorene catabolic process; IDA:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase; Plasmid.
FT CHAIN 1..357
FT /note="Fluoren-9-ol dehydrogenase"
FT /id="PRO_0000430705"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P16544"
FT BINDING 36..67
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P16544"
FT BINDING 87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P16544"
FT BINDING 202
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P16544"
SQ SEQUENCE 357 AA; 38512 MW; F17C1C65BA782575 CRC64;
MSESGGGTVA TARQRQLVER ALGEWQGEVA GRVIVVTGGA RGIGRSLCEG LLRAGAKVVA
ADLTWDDADD FRKQLESDGS GMAVDMDITD DDALDAARDA VIDRFGTVDV LVNNASLVSE
TLFPPTGHRN TLDTTDRDWE VMFGVNVFGT LKAIRRFIEP MRAQQRGSIV NVVSSGVLAV
AAGGGYHGLR PWTVEMPYQA TKAAVMALTF YLAEEVRGDG VAVNAIMPGH TRASWFDATA
RAFNEQGIAY FMRPAIPEHL LPISLFLAAQ DSAGASGRLY YVPEWNYDHG YGDYAAWQDH
ELPPDMEEIY SRLEAATPSY ERAGVAHLPF DAQGALYAAG MANLGAQNSW TSNDSAQ
