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Database: UniProt
Entry: A0A426GF25_9CAUL
LinkDB: A0A426GF25_9CAUL
Original site: A0A426GF25_9CAUL 
ID   A0A426GF25_9CAUL        Unreviewed;       299 AA.
AC   A0A426GF25;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   13-SEP-2023, entry version 11.
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:RRN62644.1};
GN   ORFNames=EIK80_21400 {ECO:0000313|EMBL:RRN62644.1};
OS   Caulobacter sp. 602-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=2492472 {ECO:0000313|EMBL:RRN62644.1, ECO:0000313|Proteomes:UP000268773};
RN   [1] {ECO:0000313|EMBL:RRN62644.1, ECO:0000313|Proteomes:UP000268773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=602-1 {ECO:0000313|EMBL:RRN62644.1,
RC   ECO:0000313|Proteomes:UP000268773};
RA   Gao J., Sun J.;
RT   "The genome of Caulobacter sp 602-1.";
RL   Submitted (NOV-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}.
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:RRN62644.1}.
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DR   EMBL; RRYI01000008; RRN62644.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A426GF25; -.
DR   OrthoDB; 9803892at2; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000268773; Unassembled WGS sequence.
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   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,
KW   ECO:0000313|EMBL:RRN62644.1}.
FT   DOMAIN          1..281
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   299 AA;  30930 MW;  044E7E8FBA1D6FBC CRC64;
     MRIALFGANG QLGSDLVTLA GRRGLDLVAV TRAQVDAADP AAGFDGLDFD IAINCVAVTR
     VDDCEKDPGP AVAVNAHFAG RLARACAVRG ARLVQVSTDY VYGGQAQREP LSEDVGRAPV
     NVYGATKALG EDLARLEHDD VIVARVASLF GVAGASGKGG NFVETMLRLA KEKGRLTVVA
     DQVMSPTASL DAGEAILDLV AAKALAGDYH VVNSGAASWC AFADAIIARA GVAAEVAPIP
     TSQFPTPARR PPYSALSNAK LVAAIGRPMP DWADALDRYL AAKGHIRAAT VKISSKSSR
//
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