KDRDH_SPHSS
ID KDRDH_SPHSS Reviewed; 249 AA.
AC Q1NEI6;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=2-dehydro-3-deoxy-L-rhamnonate dehydrogenase (NAD(+)) {ECO:0000305};
DE EC=1.1.1.401 {ECO:0000269|PubMed:19187228};
DE AltName: Full=2-keto-3-deoxy-L-rhamnonate dehydrogenase {ECO:0000303|PubMed:19187228};
DE Short=KDRDH;
DE Short=L-KDR dehydrogenase;
DE AltName: Full=L-KDR 4-dehydrogenase {ECO:0000303|PubMed:19187228};
GN Name=LRA5 {ECO:0000303|PubMed:19187228}; ORFNames=SKA58_03590;
OS Sphingomonas sp. (strain SKA58).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=314266;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA58;
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-20, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND PATHWAY.
RC STRAIN=NBRC 101715;
RX PubMed=19187228; DOI=10.1111/j.1742-4658.2009.06885.x;
RA Watanabe S., Makino K.;
RT "Novel modified version of nonphosphorylated sugar metabolism--an
RT alternative L-rhamnose pathway of Sphingomonas sp.";
RL FEBS J. 276:1554-1567(2009).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent dehydrogenation of 2-dehydro-
CC 3-deoxy-L-rhamnonate to form 2,4-didehydro-3-deoxy-L-rhamnonate. Does
CC not show any detectable activity in the presence of NADP(+).
CC {ECO:0000269|PubMed:19187228}.
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:19187228};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.65 mM for 2-dehydro-3-deoxy-L-rhamnonate
CC {ECO:0000269|PubMed:19187228};
CC KM=1.27 mM for 2-dehydro-3-deoxy-L-lyxonate
CC {ECO:0000269|PubMed:19187228};
CC KM=1.9 mM for 2-dehydro-3-deoxy-L-mannonate
CC {ECO:0000269|PubMed:19187228};
CC Note=kcat is 51.8 min(1-) with 2-dehydro-3-deoxy-L-rhamnonate as
CC substrate. kcat is 11 min(1-) with 2-dehydro-3-deoxy-L-lyxonate as
CC substrate. kcat is 0.72 min(1-) with 2-dehydro-3-deoxy-L-mannonate as
CC substrate. {ECO:0000269|PubMed:19187228};
CC -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation.
CC {ECO:0000305|PubMed:19187228}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19187228}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AAQG01000004; EAT09364.1; -; Genomic_DNA.
DR RefSeq; WP_009820502.1; NZ_CH959306.1.
DR AlphaFoldDB; Q1NEI6; -.
DR SMR; Q1NEI6; -.
DR STRING; 314266.SKA58_03590; -.
DR KEGG; ag:EAT09364; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_3_5; -.
DR BioCyc; MetaCyc:MON-16233; -.
DR BRENDA; 1.1.1.401; 5801.
DR UniPathway; UPA00541; -.
DR Proteomes; UP000005395; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0019301; P:rhamnose catabolic process; IEA:UniProtKB-UniPathway.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; NAD; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:19187228"
FT CHAIN 2..249
FT /note="2-dehydro-3-deoxy-L-rhamnonate dehydrogenase
FT (NAD(+))"
FT /id="PRO_0000438496"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
SQ SEQUENCE 249 AA; 25663 MW; D051D6BA6CEE2A48 CRC64;
MSVFAGRYAG RCAIVTGGAS GLGKQVAARI IAEGGAVALW DLNGDALAAT QAEIDATHVV
ALDVSDHAAV AAAAKDSAAA LGKVDILICS AGITGATVPV WEFPVDSFQR VIDINLNGLF
YCNREVVPFM LENGYGRIVN LASVAGKEGN PNASAYSASK AGVIGFTKSL GKELAGKGVI
ANALTPATFE SPILDQLPQS QVDYMRSKIP MGRLGLVEES AAMVCFMASE ECSFTTASTF
DTSGGRTTF