ID A0A0C2L6R0_9CYAN Unreviewed; 742 AA.
AC A0A0C2L6R0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=SD81_05635 {ECO:0000313|EMBL:KIJ78787.1};
OS Tolypothrix campylonemoides VB511288.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ78787.1};
RN [1] {ECO:0000313|EMBL:KIJ78787.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ78787.1};
RA Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT VB511288.";
RL Submitted (JAN-2015) 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|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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIJ78787.1}.
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DR EMBL; JXCB01000004; KIJ78787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2L6R0; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW NADP {ECO:0000256|RuleBase:RU364082};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364082};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 467..721
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 742 AA; 82588 MW; ACD96988E6DED584 CRC64;
MTSFNSTLEN HYSKLPPLEV WAGVECTVNR VGDEYFDQLE RNGHATRLDD LDLFAELGIK
AIRYPVLWER TAPDGLENAD WSWADERLGR LRELGINPIV GLVHHGSGPR HTSLVDPEFP
EKLALYARAV AERYPWVTHY TPVNEPLTTA RFSGMYGHWY PHGRDGLTFA RALLGECRGV
ALSMQAIREV NPNAQLVQTD DLGKIYSTPK LAYQAEFENE RRWLSFDLLC GRITPTHPMW
RYLHKCGISE AELDWFVENP CPPDIIGINH YLTSDRFLDE RKERYPTSSH GGNGRDEYAD
IEAVRVCAEG AAGPRNLLLE AWERYKLPLA VTEAHLHCTR EEQLRWLYEV WNAALQLRDQ
GVDIRAVTAW SLLGTYDWNS LVTRSVGYYE SGVFDLRSSR PRPTAIAKMI RDLSAGHKPD
HPLLETPGWW HRQERLLYPA VSCLKESSVQ PGVGGEMTPS SASSPLAIVG ARGTLGRAFA
RLCELRGISY RLLTRQEMDI ADPGTVNAVL AELKPWAVVN AAGYVRVDDA EREPHVCLRV
NAEGPAILAA ACAQHNVALL TFSSDLVFDG AVFNPYIESD TVAPLNVYGC SKALAEKLVL
KVNPASLIIR TSAFFGPWDD YNFVTIALRQ LSAGNSFVAA EDAIISPTYV PDLVHASLDL
LIDGESGLWH LANKGAIAWA DLARLAAKTA GFNPSNVIAL PTQELGLTAK RPSYSVLGSN
RGELMSSLDS AMSRYFDECQ RF
//