(data stored in SCRATCH zone)

SWISSPROT: Q144P3_PARXL

ID   Q144P3_PARXL            Unreviewed;       305 AA.
AC   Q144P3;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 76.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   ORFNames=Bxe_A3802 {ECO:0000313|EMBL:ABE29196.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE29196.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE29196.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE29196.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-
CC       hexulose to yield dTDP-L-rhamnose.
CC       {ECO:0000256|RuleBase:RU364082}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-
CC         rhamnose + H(+) + NADPH; Xref=Rhea:RHEA:21796,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57510, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:62830; EC=1.1.1.133;
CC         Evidence={ECO:0000256|RuleBase:RU364082};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU364082};
CC       Note=Binds 1 Mg(2+) ion per monomer.
CC       {ECO:0000256|RuleBase:RU364082};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC       {ECO:0000256|RuleBase:RU364082}.
CC   -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase
CC       family. {ECO:0000256|RuleBase:RU364082}.
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DR   EMBL; CP000270; ABE29196.1; -; Genomic_DNA.
DR   RefSeq; WP_011486992.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A3802; -.
DR   EnsemblBacteria; ABE29196; ABE29196; Bxe_A3802.
DR   GeneID; 4002584; -.
DR   KEGG; bxe:Bxe_A3802; -.
DR   PATRIC; fig|266265.5.peg.687; -.
DR   eggNOG; ENOG4105DBZ; Bacteria.
DR   eggNOG; COG1091; LUCA.
DR   HOGENOM; HOG000227712; -.
DR   KO; K00067; -.
DR   OMA; YHYSNEG; -.
DR   OrthoDB; 1076083at2; -.
DR   BioCyc; BXEN266265:BXE_RS03250-MONOMER; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029903; RmlD-like-bd.
DR   PANTHER; PTHR10491; PTHR10491; 1.
DR   Pfam; PF04321; RmlD_sub_bind; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01214; rmlD; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q144P3.
DR   SWISS-2DPAGE; Q144P3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   NADP {ECO:0000256|RuleBase:RU364082};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364082,
KW   ECO:0000313|EMBL:ABE29196.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN       11    303       RmlD_sub_bind. {ECO:0000259|Pfam:
FT                                PF04321}.
SQ   SEQUENCE   305 AA;  32753 MW;  100FB032BAB6AEDA CRC64;
     MRDKASSVPI LLVTGSRGQV GFELRRSLAS LGNVVALDRS VCDLRSPDSI RSVVREVQPD
     VIVNPAAYTA VDAAENDAEL AYAINGVAAG VLAEEAKSLG GLLVHYSTDY VFDGRKDGPY
     VETDVVNPQS VYGKSKLAGE QAIAERGATA IVLRTCWVAG AHGSNFAKTM LRLGRERDSL
     RVIADQYGAP TTAALIADVT AQIVARHWLH GDRAAFASGV YHLAAAGQTS WHGYATEVLQ
     FAAARGVELK VDLARIEPIA TADYPLPAPR PANSRLDTHK LRQTFGINLP DWRDGVHHLL
     EQILP
//

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