ID K9YM63_CYASC Unreviewed; 462 AA.
AC K9YM63;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN OrderedLocusNames=Cyast_2076 {ECO:0000313|EMBL:AFZ48026.1};
OS Cyanobacterium stanieri (strain ATCC 29140 / PCC 7202).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Cyanobacterium.
OX NCBI_TaxID=292563 {ECO:0000313|EMBL:AFZ48026.1, ECO:0000313|Proteomes:UP000010483};
RN [1] {ECO:0000313|Proteomes:UP000010483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29140 / PCC 7202 {ECO:0000313|Proteomes:UP000010483};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- FUNCTION: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to
CC yield dTDP-L-rhamnose. {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, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57510, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:62830; EC=1.1.1.133;
CC Evidence={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 family.
CC {ECO:0000256|ARBA:ARBA00010944, ECO:0000256|RuleBase:RU364082}.
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DR EMBL; CP003940; AFZ48026.1; -; Genomic_DNA.
DR AlphaFoldDB; K9YM63; -.
DR STRING; 292563.Cyast_2076; -.
DR KEGG; csn:Cyast_2076; -.
DR PATRIC; fig|292563.3.peg.2170; -.
DR eggNOG; COG1091; Bacteria.
DR eggNOG; COG1898; Bacteria.
DR HOGENOM; CLU_045518_6_1_3; -.
DR BioCyc; CSTA292563:G1353-2080-MONOMER; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000010483; Chromosome.
DR GO; GO:0008830; F:dTDP-4-dehydrorhamnose 3,5-epimerase activity; IEA:InterPro.
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 CDD; cd00438; cupin_RmlC; 1.
DR CDD; cd05254; dTDP_HR_like_SDR_e; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000888; RmlC-like.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR InterPro; IPR029903; RmlD-like-bd.
DR NCBIfam; TIGR01221; rmlC; 1.
DR NCBIfam; TIGR01214; rmlD; 1.
DR PANTHER; PTHR10491; DTDP-4-DEHYDRORHAMNOSE REDUCTASE; 1.
DR PANTHER; PTHR10491:SF4; METHIONINE ADENOSYLTRANSFERASE 2 SUBUNIT BETA; 1.
DR Pfam; PF00908; dTDP_sugar_isom; 1.
DR Pfam; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|RuleBase:RU364082};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364082,
KW ECO:0000313|EMBL:AFZ48026.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010483}.
FT DOMAIN 184..461
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT ACT_SITE 62
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT ACT_SITE 132
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT SITE 138
FT /note="Participates in a stacking interaction with the
FT thymidine ring of dTDP-4-oxo-6-deoxyglucose"
FT /evidence="ECO:0000256|PIRSR:PIRSR600888-3"
SQ SEQUENCE 462 AA; 52570 MW; AB8DD891381DB261 CRC64;
MELIKTNIEG VLIIKPRLFE DNRGWFMETY ADQKLKEKGI NIKFVQDNHS LSLQKDTLRG
LHFQVNPKAQ TKLVRCTRGS ILDVAVDLRK GSPTFKKWVS VELSAENKKQ LLIPKGFAHG
FLTLTDDAEV QYKVDEYYNP ECDRTLKFND PDLGINWQIE NPILSEKDLT APLLKDSDVN
FQIKILVTGS NGQLGYDVIQ DLSQIGVKII ATTKNDFDIT NPTQTKQCIS DINPDIIIHC
AAYTAVDQAE EEKDICYSVN VEGTKNIAQI AQEINAKLVY ISTDYVFDGS GNNPHLITDS
INPLNHYGYT KAQGEEVIRN LIQRHFIIRT SWVYGINGNN FVKTMIRLAK SKKTIQVVND
QIGSPTYTKD LARFISKLIQ TDNYGTYHGV NEGYCSWWQF AQEIFAQLST NIEVIPISSQ
DYITKAQRPL NSRLSTVNIE NIGLQKLPHW KNALTRYLQE IQ
//
