PLH6_FORAG
ID PLH6_FORAG Reviewed; 264 AA.
AC T2KLZ8;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase {ECO:0000305};
DE EC=1.1.1.127 {ECO:0000250|UniProtKB:P37769};
DE AltName: Full=2-deoxy-D-gluconate 3-dehydrogenase {ECO:0000303|PubMed:31285597};
DE AltName: Full=2-keto-3-deoxygluconate 5-dehydrogenase;
DE AltName: Full=2-keto-3-deoxygluconate oxidoreductase;
DE Short=KDG oxidoreductase;
DE AltName: Full=P6_dehydrogenase {ECO:0000303|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P6 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P6;
GN Name=kduD; ORFNames=BN863_21950;
OS Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 /
OS M-2Alg 35-1).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1347342;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1;
RX PubMed=23995932; DOI=10.1128/aem.01937-13;
RA Mann A.J., Hahnke R.L., Huang S., Werner J., Xing P., Barbeyron T.,
RA Huettel B., Stueber K., Reinhardt R., Harder J., Gloeckner F.O.,
RA Amann R.I., Teeling H.;
RT "The genome of the alga-associated marine flavobacterium Formosa agariphila
RT KMM 3901T reveals a broad potential for degradation of algal
RT polysaccharides.";
RL Appl. Environ. Microbiol. 79:6813-6822(2013).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=31285597; DOI=10.1038/s41589-019-0311-9;
RA Reisky L., Prechoux A., Zuehlke M.K., Baeumgen M., Robb C.S., Gerlach N.,
RA Roret T., Stanetty C., Larocque R., Michel G., Song T., Markert S.,
RA Unfried F., Mihovilovic M.D., Trautwein-Schult A., Becher D., Schweder T.,
RA Bornscheuer U.T., Hehemann J.H.;
RT "A marine bacterial enzymatic cascade degrades the algal polysaccharide
RT ulvan.";
RL Nat. Chem. Biol. 15:803-812(2019).
CC -!- FUNCTION: 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase involved in
CC ulvan degradation (Probable). Ulvan is the main polysaccharide
CC component of the Ulvales (green seaweed) cell wall. It is composed of
CC disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S)
CC linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose
CC (Xyl) (Probable). Catalyzes the reversible reduction of 2,5-diketo-3-
CC deoxygluconate (DKII or 4,6-dihydroxy-2,5-dioxohexanoate) into 2-keto-
CC 3-deoxygluconate (KDG or 2-dehydro-3-deoxygluconate) with a concomitant
CC oxidation of NADH (By similarity). {ECO:0000250|UniProtKB:P37769,
CC ECO:0000305|PubMed:31285597}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-D-gluconate + NAD(+) = 3-deoxy-D-glycero-
CC 2,5-hexodiulosonate + H(+) + NADH; Xref=Rhea:RHEA:24232,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29071, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:57990; EC=1.1.1.127;
CC Evidence={ECO:0000250|UniProtKB:P37769};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P37769}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31285597}.
CC -!- INDUCTION: By ulvan and rhamnose. {ECO:0000269|PubMed:31285597}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG315671; CDF79907.1; -; Genomic_DNA.
DR RefSeq; WP_038530495.1; NZ_HG315671.1.
DR AlphaFoldDB; T2KLZ8; -.
DR SMR; T2KLZ8; -.
DR STRING; 1347342.BN863_21950; -.
DR EnsemblBacteria; CDF79907; CDF79907; BN863_21950.
DR PATRIC; fig|1347342.6.peg.2202; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_1_10; -.
DR OMA; FSSISYM; -.
DR OrthoDB; 1294334at2; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047001; F:2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cytoplasm; NAD; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..264
FT /note="2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase"
FT /id="PRO_0000448309"
FT ACT_SITE 160
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 14..38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P37769"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P37769"
SQ SEQUENCE 264 AA; 27957 MW; 413DD93C7C59A547 CRC64;
MSVDLFDVKG KIALVTGSTH GLGMAMAKGL GLAGATIVVN GNSSQDKIDS AIAEYEKEGI
KAVGYKFNVA KEDEVQAAVS KIEAEVGPID ILINNAGIIK RTPLLEMEVA DFKEVVDIDL
VSPFIVSKHV VKNMVERKAG KVINICSMMS ELGRNSVGAY AAAKGGLKML TQNMATEWAK
YNIQVNGIGP GYFATSQTAP IRVDGHPFND FIINRTPAAK WGDPNDLAGA AIFLSSKASD
FVNGHVVYVD GGILATIGKP SNEE
