ID R5Q0Z7_9PROT Unreviewed; 273 AA.
AC R5Q0Z7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|ARBA:ARBA00017099};
DE EC=1.1.1.133 {ECO:0000256|ARBA:ARBA00012929};
DE AltName: Full=dTDP-4-keto-L-rhamnose reductase {ECO:0000256|ARBA:ARBA00033299};
DE AltName: Full=dTDP-6-deoxy-L-lyxo-4-hexulose reductase {ECO:0000256|ARBA:ARBA00030715};
DE AltName: Full=dTDP-6-deoxy-L-mannose dehydrogenase {ECO:0000256|ARBA:ARBA00033463};
DE AltName: Full=dTDP-L-rhamnose synthase {ECO:0000256|ARBA:ARBA00029600};
GN ORFNames=BN820_00905 {ECO:0000313|EMBL:CCZ22148.1};
OS Acetobacter sp. CAG:977.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=1262685 {ECO:0000313|EMBL:CCZ22148.1, ECO:0000313|Proteomes:UP000018259};
RN [1] {ECO:0000313|EMBL:CCZ22148.1, ECO:0000313|Proteomes:UP000018259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:977 {ECO:0000313|Proteomes:UP000018259};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004781}.
CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC {ECO:0000256|ARBA:ARBA00010944}.
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:CCZ22148.1}.
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DR EMBL; CAZQ010000074; CCZ22148.1; -; Genomic_DNA.
DR AlphaFoldDB; R5Q0Z7; -.
DR STRING; 1262685.BN820_00905; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000018259; Unassembled WGS sequence.
DR GO; GO:0003909; F:DNA ligase activity; IEA:InterPro.
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; IPR016059; DNA_ligase_ATP-dep_CS.
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.
DR PROSITE; PS00697; DNA_LIGASE_A1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000018259}.
FT DOMAIN 2..272
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 273 AA; 30321 MW; 2F4BA6BAFCC111E5 CRC64;
MLLVTGANGQ LGTELRALLP QALFADLPDL DITDESAVAE FVKAENIDTI INAAAYTAVE
KAEDDPDLCY KVNVIGPMNL AKTGAKIIHV STDYVFDGKS YLPYKETDAT NPESVYGQTK
RDGERAVMDL SSTCAIFRTA WLYSPYGNNF VKTMRRLGAE RESINVVFDQ IGTPTYAFDL
AQAIVAALPQ IKDGTHEIYH CSDEGAASWY DFTCEIMRLS GLKCRVNPIT TDQYPTKAKR
PFYSVLNKAK IKSTFGISIP HWQESLEKCL KKF
//
