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Database: UniProt
Entry: Q93FF7_ACICA
LinkDB: Q93FF7_ACICA
Original site: Q93FF7_ACICA 
ID   Q93FF7_ACICA            Unreviewed;       297 AA.
AC   Q93FF7;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 61.
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   Name=rfbD {ECO:0000313|EMBL:AAL26873.1};
OS   Acinetobacter calcoaceticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=471 {ECO:0000313|EMBL:AAL26873.1};
RN   [1] {ECO:0000313|EMBL:AAL26873.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Eun S.H., Kim D.J., Kim Y.S.;
RT   "Acinetobacter calcoaceticus rfbB gene for dTDP-D-glucose-4,6-dehydratase,
RT   rfbD gene for dTDP-rhamnose synthetase, rfbA gene for glucose-1-phosphate
RT   thymidylyltransferase, and rfbC gene for dTDP-6-deoxy-D-glucose-3,5-
RT   epimerase.";
RL   Submitted (OCT-2000) 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; AF315583; AAL26873.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93FF7; -.
DR   UniPathway; UPA00124; -.
DR   UniPathway; UPA00281; -.
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   GO; GO:0009243; P:O antigen 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}.
FT   DOMAIN          1..294
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   297 AA;  32207 MW;  3B3ED0C50C248967 CRC64;
     MKILLLGKNG QVGWELQRAL APLGEVIALD RHGLNGLSGD MTQPQAISDT ILAVQPDVVV
     NASAYTAVDL AETERELADV VNHQTVMAVA KACQHVNALF VHYSTDYVFD GVGETAFVET
     DAIAPLNVYG KTKALGEQAI VQSGCQYLIF RTSWVYASKG KNFLKTMLGL AQQREELSII
     ADQIGAPTSA ELIADVTAHA IPQTLTDKSK VGTYHLVASG ETSWFGYASF VFEQVRAFGQ
     ALTIQNVNAI PTSAYPTPAT RPHNSRLNNQ KIQHTFGILL PNWQDGVKRA LVELLSK
//
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