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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
 
 
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