ID B8HTF6_CYAP4 Unreviewed; 738 AA.
AC B8HTF6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN OrderedLocusNames=Cyan7425_2019 {ECO:0000313|EMBL:ACL44382.1};
OS Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Cyanothecaceae;
OC Cyanothece.
OX NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL44382.1};
RN [1] {ECO:0000313|EMBL:ACL44382.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCC 7425 {ECO:0000313|EMBL:ACL44382.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Liberton M., Stoeckel J., Banerjee A., Singh A., Page L.,
RA Sato H., Zhao L., Sherman L., Pakrasi H., Richardson P.;
RT "Complete sequence of chromosome Cyanothece sp. PCC 7425.";
RL Submitted (JAN-2009) 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}.
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DR EMBL; CP001344; ACL44382.1; -; Genomic_DNA.
DR AlphaFoldDB; B8HTF6; -.
DR STRING; 395961.Cyan7425_2019; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; cyn:Cyan7425_2019; -.
DR eggNOG; COG1091; Bacteria.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_023233_0_0_3; -.
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 ECO:0000313|EMBL:ACL44382.1}; Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 460..714
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 738 AA; 82830 MW; B8E149A1A1B19D4F CRC64;
MHTQANALPA LELWGGVECT VNRVGDRYFD QLERSGHACR IADLDLFASL GIRGIRYPLL
WERIAPHGLE TANWEWADQR LQRLRDLGIR PIVGLVHHGS GPAHTSLSDP SFPHQLAQYA
QAVAERYPWI DAYTPINEPL TTARFSGLYG HWYPHGQDDR TFLQVLLHQC QAITLAMQAI
RQINPQAQLV QTEDLGKTYS TPLLADQAEF ENERRWLSFD LLFGRVNPQH PLWKYFIKSG
IDPIQLEPFQ SQPCPPNILG INHYLTSERW LDEHLDHYPE HFHGGNGQHT YADVEAVRVC
AEGLAGHGQL LREVWERYGQ SGENGPAIAV TEVHLGCTRE EQLRWLDQVW QSAQDLRSQG
VKLVAITAWS LLGAYDWNSL VTRDAGFYEP GVFDLRSPTP RATALAWMLR YLSEGRRYDH
PLLLVPGWWQ RPERLHYPTV NCFQNPVARG QQAIIPTPPV LITGATGTLG RAFARICQLR
GIPYRLLGRR EMDITNPVSV NQVLEELQPW AVINTAGYVR VDDAEREAHL CRQINTDGAA
ILAQACVDRN TAYVTFSSDL VFDGQQADPY VESCAVAPLN VYGDSKAIAE QWVLQTHPCA
LVIRTSAFFG PWDEYNFVTL LRRHLAAGQP FRAADDAIVS PTYVPDLVHI ALDLLIDGEA
GLWHLANPGA VSWAELALCV AEQARLDATL IQPLPTRALG LLAQRPAYSV LGSERGNLLP
CLSQGLDRYL TECEISCH
//
