ID Q8L347_VIBCL Unreviewed; 290 AA.
AC Q8L347;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 63.
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};
OS Vibrio cholerae O37.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=185332 {ECO:0000313|EMBL:AAM22596.1};
RN [1] {ECO:0000313|EMBL:AAM22596.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1322-69 {ECO:0000313|EMBL:AAM22596.1};
RX PubMed=11953381; DOI=10.1128/IAI.70.5.2441-2453.2002;
RA Li M., Shimada T., Morris J.G. Jr, Sulakvelidze A., Sozhamannan S.;
RT "Evidence for the emergence of non-O1 and non-O139 Vibrio cholerae strains
RT with pathogenic potential by exchange of O-antigen biosynthesis regions.";
RL Infect. Immun. 70:2441-2453(2002).
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; AF390573; AAM22596.1; -; Genomic_DNA.
DR RefSeq; WP_000697976.1; NZ_CP047305.1.
DR AlphaFoldDB; Q8L347; -.
DR KEGG; ag:AAM22596; -.
DR BioCyc; MetaCyc:MONOMER-18156; -.
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 InterPro; IPR005913; dTDP_dehydrorham_reduct.
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; 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..224
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 290 AA; 32801 MW; 1C7B32C146B3ABE1 CRC64;
MKILIVGTTG MLGYSLFTNL SEHDGYEVFG TVRNILGKEK FFEEYLDNLI FDIDVNDFSR
LKFAIETIKP DVVINCIGLI KQHDISKQHI NAIEINSLLP HKIAQVCDGI SAKLIHFSTD
CVFSGKTGKY IEADIPDATD IYGKSKCLGE VNYGKHLTLR TSIIGHELNT SVSLIDWFLT
QNNKVNGFSK AVFSGLPTCY IANILIKYIL PNKQLNGLFH LSVDPIDKYS LLKLISKVYG
KGIEVIKSEH LVIDRSLDSS YLRNKTGLNT IDWPELINYM YADYLKRYCK
//
