ID Q8RIB0_FUSNN Unreviewed; 298 AA.
AC Q8RIB0;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN OrderedLocusNames=FN1698 {ECO:0000313|EMBL:AAL93813.1};
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=190304 {ECO:0000313|EMBL:AAL93813.1, ECO:0000313|Proteomes:UP000002521};
RN [1] {ECO:0000313|EMBL:AAL93813.1, ECO:0000313|Proteomes:UP000002521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 /
RC KCTC 2640 / LMG 13131 / VPI 4355 {ECO:0000313|Proteomes:UP000002521};
RX PubMed=11889109; DOI=10.1128/JB.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N., Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(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|RuleBase:RU364082};
CC -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC {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; AE009951; AAL93813.1; -; Genomic_DNA.
DR RefSeq; NP_602514.1; NC_003454.1.
DR RefSeq; WP_011015768.1; NZ_CP028101.1.
DR AlphaFoldDB; Q8RIB0; -.
DR STRING; 190304.FN1698; -.
DR PaxDb; 190304-FN1698; -.
DR EnsemblBacteria; AAL93813; AAL93813; FN1698.
DR GeneID; 79784479; -.
DR KEGG; fnu:FN1698; -.
DR PATRIC; fig|190304.8.peg.188; -.
DR eggNOG; COG1091; Bacteria.
DR HOGENOM; CLU_045518_1_2_0; -.
DR InParanoid; Q8RIB0; -.
DR BioCyc; FNUC190304:G1FZS-200-MONOMER; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000002521; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IBA:GO_Central.
DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IBA:GO_Central.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IBA:GO_Central.
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:AAL93813.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002521}.
FT DOMAIN 3..295
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 298 AA; 33988 MW; 35B7EB4557F7B591 CRC64;
MKLIFGANGK LGTDFKELFD SIGEKYIATD KDEVDITNGD FLRAYIKTMH QNYKIDTIIN
CAAYNDVDKA ETEKELCYKA NAEAPANLAM IASEIGATYI TYSTDFVFNG MTTNYLYNES
TGYTEEDEAH PLSAYAKAKY EGELLVSQII ENPENTSRIY IVRTSWVFGK GGMNFVEKII
ELSKEKDELK VVDDQVSSPT YSKDLAYFSW ELIKKGCESG VYHLTNDSIV SKYEEAQYIL
EKISWKGNLI RAKSEDFNLL AERPKFSKLS CKKIKEKLGV SIPNWKDAID RYFKENNK
//
