ID E1QZA1_OLSUV Unreviewed; 481 AA.
AC E1QZA1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN OrderedLocusNames=Olsu_0600 {ECO:0000313|EMBL:ADK67715.1};
OS Olsenella uli (strain ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 /
OS NCIMB 702895 / VPI D76D-27C) (Lactobacillus uli).
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=633147 {ECO:0000313|EMBL:ADK67715.1, ECO:0000313|Proteomes:UP000000333};
RN [1] {ECO:0000313|EMBL:ADK67715.1, ECO:0000313|Proteomes:UP000000333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 / NCIMB 702895 /
RC VPI D76D-27C {ECO:0000313|Proteomes:UP000000333};
RX PubMed=21304694; DOI=10.4056/sigs.1082860;
RA Goker M., Held B., Lucas S., Nolan M., Yasawong M., Glavina Del Rio T.,
RA Tice H., Cheng J.F., Bruce D., Detter J.C., Tapia R., Han C., Goodwin L.,
RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Rohde M., Sikorski J., Pukall R., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Olsenella uli type strain (VPI D76D-27C).";
RL Stand. Genomic Sci. 3:76-84(2010).
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 3,5-epimerase family.
CC {ECO:0000256|ARBA:ARBA00010154}.
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; CP002106; ADK67715.1; -; Genomic_DNA.
DR RefSeq; WP_013251467.1; NZ_JQCO01000001.1.
DR AlphaFoldDB; E1QZA1; -.
DR STRING; 633147.Olsu_0600; -.
DR GeneID; 78512027; -.
DR KEGG; ols:Olsu_0600; -.
DR PATRIC; fig|633147.7.peg.952; -.
DR eggNOG; COG1091; Bacteria.
DR eggNOG; COG1898; Bacteria.
DR HOGENOM; CLU_045518_6_2_11; -.
DR OMA; IGEGRNF; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000000333; Chromosome.
DR GO; GO:0008830; F:dTDP-4-dehydrorhamnose 3,5-epimerase 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; 2.60.120.10; Jelly Rolls; 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; IPR000888; RmlC-like.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_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; PF00908; dTDP_sugar_isom; 1.
DR Pfam; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:ADK67715.1};
KW NADP {ECO:0000256|RuleBase:RU364082};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364082,
KW ECO:0000313|EMBL:ADK67715.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000333}.
FT DOMAIN 189..478
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT ACT_SITE 132
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT SITE 138
FT /note="Participates in a stacking interaction with the
FT thymidine ring of dTDP-4-oxo-6-deoxyglucose"
FT /evidence="ECO:0000256|PIRSR:PIRSR600888-3"
SQ SEQUENCE 481 AA; 53766 MW; 9D9BD414915EE81E CRC64;
MDFEKDLRSF GTEIAGLRVF DLCVHGDDRG WFKENWQQAK MSSCGLPDFH PVQNNISFNA
QRGVTRGIHA EPWDKYISVA SGSIFGVWVD LRAGEGFGRV FSCRIDPSKA VFVPRGVGNA
FQALEDGTVY TYLVNAHWSQ ELKESYTFVN LADEQLAIEW PIPLSECELS QADRDHPALR
DVSPMQGKRT LVTGCNGQLG RAVRQLANER KLVGFDYCDI DTFDFSDIRS YDDIPWDAYG
AVINCGAYTA VDRAESPEGR VMCWKANALG PSLLTQTCAR HGITLVHVSS EYVFDGSREL
HDEDETYAPL SVYGQSKAAG DIALSCCPKY YIVRTSWVIG DGHNFVKTMA RLSDRCADPA
DSLDSVSVVN DQLGRPTFAD ELARGIFWLL DTRPAYGIYN LSNAGRIASW YDIARRTFEM
RNGNGHCVHA TSTADYYAGS EAPVACRPRN SALSLEKMCR LGFEPRDWEG QLSSYMRRCE
R
//