KDRDH_SULTA
ID KDRDH_SULTA Reviewed; 331 AA.
AC P0DOW0;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=2-dehydro-3-deoxy-L-rhamnonate dehydrogenase (NAD(+)) {ECO:0000305};
DE EC=1.1.1.401 {ECO:0000269|PubMed:25617114};
DE AltName: Full=2-keto-3-deoxy-L-rhamnonate dehydrogenase {ECO:0000303|PubMed:25617114};
DE Short=KDRDH {ECO:0000303|PubMed:25617114};
DE Short=L-KDR dehydrogenase {ECO:0000303|PubMed:25617114};
GN OrderedLocusNames=Sulth_3557 {ECO:0000303|PubMed:25617114};
OS Sulfobacillus thermosulfidooxidans (strain DSM 9293 / VKM B-1269 / AT-1).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales;
OC Clostridiales Family XVII. Incertae Sedis; Sulfobacillus.
OX NCBI_TaxID=929705;
RN [1]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RC STRAIN=DSM 9293 / VKM B-1269 / AT-1;
RX PubMed=25617114; DOI=10.1007/s00792-015-0731-8;
RA Bae J., Kim S.M., Lee S.B.;
RT "Identification and characterization of 2-keto-3-deoxy-L-rhamnonate
RT dehydrogenase belonging to the MDR superfamily from the thermoacidophilic
RT bacterium Sulfobacillus thermosulfidooxidans: implications to L-rhamnose
RT metabolism in archaea.";
RL Extremophiles 19:469-478(2015).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent dehydrogenation of 2-dehydro-
CC 3-deoxy-L-rhamnonate to 2,4-didehydro-3-deoxy-L-rhamnonate. Also has
CC weak dehydrogenase activity on butane-2,3-diol. Does not show any
CC detectable activity in the presence of NADP(+).
CC {ECO:0000269|PubMed:25617114}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-L-rhamnonate + NAD(+) = 2,4-didehydro-3-
CC deoxy-L-rhamnonate + H(+) + NADH; Xref=Rhea:RHEA:36499,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58371, ChEBI:CHEBI:131847; EC=1.1.1.401;
CC Evidence={ECO:0000269|PubMed:25617114};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O58389};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:O58389};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.0 mM for 2-dehydro-3-deoxy-L-rhamnonate
CC {ECO:0000269|PubMed:25617114};
CC KM=14.8 mM for butane-2,3-diol {ECO:0000269|PubMed:25617114};
CC KM=0.42 mM for NAD(+) {ECO:0000269|PubMed:25617114};
CC Vmax=12.8 umol/min/mg enzyme with 2-dehydro-3-deoxy-L-rhamnonate as
CC substrate {ECO:0000269|PubMed:25617114};
CC Vmax=12.8 umol/min/mg enzyme with butane-2,3-diol as substrate
CC {ECO:0000269|PubMed:25617114};
CC pH dependence:
CC Optimum pH is 9.5. {ECO:0000269|PubMed:25617114};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:25617114};
CC -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation.
CC {ECO:0000305|PubMed:25617114}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- CAUTION: The sequence shown here has been extracted from the
CC Sulfobacillus thermosulfidooxidans DSM 9293 genome sequencing
CC BioProject (Accession PRJNA61271, JGI sequencing center).
CC {ECO:0000305}.
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DR AlphaFoldDB; P0DOW0; -.
DR SMR; P0DOW0; -.
DR BRENDA; 1.1.1.401; 9684.
DR UniPathway; UPA00541; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019301; P:rhamnose catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1..331
FT /note="2-dehydro-3-deoxy-L-rhamnonate dehydrogenase
FT (NAD(+))"
FT /id="PRO_0000438495"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 251..253
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT SITE 141
FT /note="Important for catalytic activity for the proton
FT relay mechanism but does not participate directly in the
FT coordination of zinc atom"
FT /evidence="ECO:0000250|UniProtKB:O58389"
SQ SEQUENCE 331 AA; 35695 MW; 8677823E3B720689 CRC64;
MKTLTWTAKE TMSILSAPAP VPEPGWIALR VAGVGICGSE LSGYLGHNEL RKPPLVMGHE
FSGVVEEVGH GVTNVKIGDL VTANPLVTCG RCIHCLRGER QRCESRRIIG IDFPGAYAER
VLVPSNQCYA VKDAIDGALV EPLACAVRAV GLARIKVGDT AVVIGAGIIG LMTVRLLGLS
GAKRIAVVDP NDERLKISQL WGATEMAPNL GALLTDNHPQ SFDCVIDAVG LSTTRRDSLN
ALIRGGRAVW IGLHEALTHL DGNQIVRDEL EVRGSFCYTD DEFIRAVSLI NSQKFLPVDR
QWLDVRSLEE GPAAFKELVN GSPFSKIILT F
