ID A0A2S2CWU5_9PROT Unreviewed; 760 AA.
AC A0A2S2CWU5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=DEW08_21920 {ECO:0000313|EMBL:AWK88747.1};
OS Azospirillum thermophilum.
OG Plasmid unnamed1 {ECO:0000313|EMBL:AWK88747.1,
OG ECO:0000313|Proteomes:UP000245629}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=2202148 {ECO:0000313|EMBL:AWK88747.1, ECO:0000313|Proteomes:UP000245629};
RN [1] {ECO:0000313|Proteomes:UP000245629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFH 70021 {ECO:0000313|Proteomes:UP000245629};
RC PLASMID=unnamed1 {ECO:0000313|Proteomes:UP000245629};
RA Zhao Z.;
RT "Azospirillum thermophila sp. nov., a novel isolated from hot spring.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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; CP029356; AWK88747.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S2CWU5; -.
DR KEGG; azz:DEW08_21920; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000245629; Plasmid unnamed1.
DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05254; dTDP_HR_like_SDR_e; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 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; IPR001360; Glyco_hydro_1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029903; RmlD-like-bd.
DR PANTHER; PTHR10491; DTDP-4-DEHYDRORHAMNOSE REDUCTASE; 1.
DR PANTHER; PTHR10491:SF4; METHIONINE ADENOSYLTRANSFERASE 2 SUBUNIT BETA; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR Pfam; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 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 Plasmid {ECO:0000313|EMBL:AWK88747.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245629}.
FT DOMAIN 449..702
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT REGION 729..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 760 AA; 83905 MW; B7711F663BA379B8 CRC64;
MPDIEIWGGL ECTVARIRDA YVDQTLLNGH EHRPEDLDRF ASLGITRLRY PVLWERVAPD
GFDRADWRWT DERLTRLRDL GIKPIVTLVH HGSGPRNTSL LDPDFATGVG RFAGMVAGRY
PWVDAYTPVN EPLTTARFSG LYGLWYPHLR DEAAFLRMLV TETRATRLAM AAIRRVNPDA
LLIQTEDLAK IHATPPLAAA AEMQNQRRWL SLDLLTGRVT PDHPFWPRLR DAGLAEEIAG
FVADPCPPDI IGFNHYLSSE RCLDHRVHRY RGLGRSRDGS NGHIDVEAVS LMAEGPTGPG
GLLREAWERY RLPMAVTEVH NGSTREDQLR WLYEVWQDAR SLAAEGVDLR AVTVWSLLGS
YDWDQLLTRC VGYYEAGPFD VRAPVPRETA LARMVRRMAD GGAVDHPVLD GPGRWHRADR
FRWRPVRCRP DVPDRPIPSW HRRPEDARRL LIVGATGTLG RAFARVAARR GLAHHPAGRG
EVDIADPASV QAALLRHRPW AVINAAGFVR VDEAEADGRR CRRENAEGPA VLAAACAAAG
IPLVGFSSDL VFDGTKRASY VEEDAVCPLN VYGETKVAAE RAIAATERGL VVRTGAFFGP
WDDHNFITTA LRRMEQGLPV AAAEDVTVSP TYVPDLVNTV LELLIDGERG IWHLASAGAV
TWAELAREAA RRAGLDAGLV RALPGEELGW AARRPRYSVL GSGRASLMPP LDDALGAFFH
AWREERRRSA APASAVLPPP GPETRSAPTP SVSPACDAAE
//
