ID A0A1W6SL73_9PROT Unreviewed; 300 AA.
AC A0A1W6SL73;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|ARBA:ARBA00017099, ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|ARBA:ARBA00012929, ECO:0000256|RuleBase:RU364082};
GN ORFNames=EBAPG3_001375 {ECO:0000313|EMBL:ARO86543.1};
OS Nitrosospira lacus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=1288494 {ECO:0000313|EMBL:ARO86543.1, ECO:0000313|Proteomes:UP000012179};
RN [1] {ECO:0000313|EMBL:ARO86543.1, ECO:0000313|Proteomes:UP000012179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APG3 {ECO:0000313|EMBL:ARO86543.1,
RC ECO:0000313|Proteomes:UP000012179};
RX PubMed=25336720; DOI=10.1099/ijs.0.070789-0;
RA Urakawa H., Garcia J.C., Nielsen J.L., Le V.Q., Kozlowski J.A., Stein L.Y.,
RA Lim C.K., Pommerening-Roser A., Martens-Habbena W., Stahl D.A., Klotz M.G.;
RT "Nitrosospira lacus sp. nov., a psychrotolerant, ammonia-oxidizing
RT bacterium from sandy lake sediment.";
RL Int. J. Syst. Evol. Microbiol. 65:242-250(2015).
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|ARBA:ARBA00000079,
CC 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. {ECO:0000256|RuleBase:RU364082};
CC -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004781, 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; CP021106; ARO86543.1; -; Genomic_DNA.
DR RefSeq; WP_040853164.1; NZ_CP021106.3.
DR AlphaFoldDB; A0A1W6SL73; -.
DR KEGG; nlc:EBAPG3_001375; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000012179; Chromosome.
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; cd05254; dTDP_HR_like_SDR_e; 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; IPR029903; RmlD-like-bd.
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; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|RuleBase:RU364082};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364082};
KW Reference proteome {ECO:0000313|Proteomes:UP000012179}.
FT DOMAIN 1..295
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 300 AA; 32739 MW; 5ACF6822F2D7DF72 CRC64;
MKILLFGKDG QVGWELQRSL APLGELVALD FDSKELCGDF TRLDGIAETV RAIAPDVVVN
AAAHTAVDKA ESEAERVRVI NALAPAALAR ECRKLGAWLV HYSTDYVFDG SGSKPWVETD
TAFPLNVYGS TKLEGEVAIL ASGCNHLIFR TSWVFAARGG NFAKTMLRLA RERERLTVID
DQIGAPTGGD LLADVTAHAI RKALRQQSVS GLYHLVAAGE TSWYGYARFV LNLAHQMGVR
LRVAPESIQP IPASAFPSPA PRPANSRLDT RKLRNTFDLS LPLWQTGVAR MLTEILETQS
//
