FCDH_PSESP
ID FCDH_PSESP Reviewed; 329 AA.
AC Q52472;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=D-threo-aldose 1-dehydrogenase {ECO:0000303|Ref.2};
DE EC=1.1.1.122 {ECO:0000269|Ref.2};
DE AltName: Full=L-fucose dehydrogenase {ECO:0000312|EMBL:BAA06803.1};
GN Name=fdh {ECO:0000303|PubMed:7765723};
OS Pseudomonas sp.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=306;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA06803.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-31; 147-171;
RP 181-195 AND 199-214.
RC STRAIN=No. 1143 {ECO:0000269|PubMed:7765723};
RX PubMed=7765723; DOI=10.1271/bbb.58.2281;
RA Yamamoto-Otake H., Nakano E., Koyama Y.;
RT "Cloning and sequencing of the L-fucose dehydrogenase gene from Pseudomonas
RT sp. No. 1143.";
RL Biosci. Biotechnol. Biochem. 58:2281-2282(1994).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=No. 1143 {ECO:0000269|Ref.2};
RA Horiuchi T., Suzuki T., Hiruma M., Saito N.;
RT "Purification and characterization of L-fucose (L-galactose) dehydrogenase
RT from Pseudomonas sp. No. 1143.";
RL Agric. Biol. Chem. 53:1493-1501(1989).
CC -!- FUNCTION: Catalyzes the oxidation of L-fucose to L-fuconolactone in the
CC presence of NADP(+). Also active against L-galactose and, to a much
CC lesser degree, D-arabinose. Uses NADP(+) as a hydrogen acceptor much
CC more efficiently than NAD(+). {ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-threo-aldose + NAD(+) = a D-threo-aldono-1,5-lactone +
CC H(+) + NADH; Xref=Rhea:RHEA:19645, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:27378, ChEBI:CHEBI:28991, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.1.1.122; Evidence={ECO:0000269|Ref.2};
CC -!- ACTIVITY REGULATION: Inhibited strongly by Hg(2+), Cd(2+) and para-
CC chloromercuribenzoic acid (PCMB) and weakly by Zn(2+) and
CC iodoacetamide. Also inhibited strongly by L-xylose but not D-glucose.
CC {ECO:0000269|Ref.2}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=280 nm {ECO:0000269|Ref.2};
CC Note=Exhibits a shoulder at 289 nm, but the characteristic absorption
CC spectrum caused by prosthetic group is not observed.
CC {ECO:0000269|Ref.2};
CC Kinetic parameters:
CC KM=1.9 mM for L-fucose (at 37 degrees Celsius) {ECO:0000269|Ref.2};
CC KM=19 mM for L-galactose (at 37 degrees Celsius) {ECO:0000269|Ref.2};
CC KM=300 mM for D-arabinose (at 37 degrees Celsius)
CC {ECO:0000269|Ref.2};
CC KM=0.016 mM for NADP(+) (at 37 degrees Celsius) {ECO:0000269|Ref.2};
CC KM=5.6 mM for NAD(+) (at 37 degrees Celsius) {ECO:0000269|Ref.2};
CC Vmax=426 umol/min/mg enzyme toward L-fucose {ECO:0000269|Ref.2};
CC Vmax=886 umol/min/mg enzyme toward L-galactose {ECO:0000269|Ref.2};
CC Vmax=132 umol/min/mg enzyme toward D-arabinose {ECO:0000269|Ref.2};
CC Vmax=366 umol/min/mg enzyme with NADP(+) and L-fucose as substrates
CC {ECO:0000269|Ref.2};
CC Vmax=24.9 umol/min/mg enzyme with NAD(+) and L-fucose as substrates
CC {ECO:0000269|Ref.2};
CC pH dependence:
CC Optimum pH is 9-10.5. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 37-40 degrees Celsius. Activity decreases at
CC 50 degrees Celsius. {ECO:0000269|Ref.2};
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000255}.
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DR EMBL; D32042; BAA06803.1; -; Genomic_DNA.
DR PIR; JC2405; JC2405.
DR AlphaFoldDB; Q52472; -.
DR SMR; Q52472; -.
DR GO; GO:0047834; F:D-threo-aldose 1-dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd19162; AKR_FDH; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044477; FDH-like.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR42686; PTHR42686; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NAD; NADP; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7765723"
FT CHAIN 2..329
FT /note="D-threo-aldose 1-dehydrogenase"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000413583"
FT ACT_SITE 58
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P06632"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06632"
SQ SEQUENCE 329 AA; 35598 MW; 4DE6F83934F709DF CRC64;
MSSTEPAAAA AGLAIPALGY GAANVGNLFR ALSDDEAWAV LEAAWDAGIR YYDTAPHYGL
GLSEKRLGAF LQTKPRDEFV VSTKAGRLLR PNPERRPSGL DTDNDFHVPD DLRREWDFTE
QGIRASIAES QERLGLDRID LLYLHDPERH DLDLALASAF PALEKVRAEG VVKAIGIGSM
VSDALTRAVR EADLDLIMVA GRYTLLEQPA ATEVLPACAE NATGIVAASV FNSGLLAQSE
PKRDGRYEYG QLPDELWDRL VRIAAICRNH DVPLPAAAIQ FPLQSALVRS VVVGGSRPAQ
LTQNAEYAAL EIPAGLWAEL AEARLIPTP
