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Database: UniProt
Entry: A0A0C2L6R0_9CYAN
LinkDB: A0A0C2L6R0_9CYAN
Original site: A0A0C2L6R0_9CYAN 
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
//
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