ID A4G488_HERAR Unreviewed; 284 AA.
AC A4G488;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
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 OrderedLocusNames=HEAR1146 {ECO:0000313|EMBL:CAL61325.1};
OS Herminiimonas arsenicoxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL61325.1, ECO:0000313|Proteomes:UP000006697};
RN [1] {ECO:0000313|EMBL:CAL61325.1, ECO:0000313|Proteomes:UP000006697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA Lett M.C., Danchin A., Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT environments.";
RL PLoS Genet. 3:518-530(2007).
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; CU207211; CAL61325.1; -; Genomic_DNA.
DR AlphaFoldDB; A4G488; -.
DR STRING; 204773.HEAR1146; -.
DR KEGG; har:HEAR1146; -.
DR eggNOG; COG1091; Bacteria.
DR HOGENOM; CLU_045518_2_2_4; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000006697; Chromosome.
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 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,
KW ECO:0000313|EMBL:CAL61325.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006697}.
FT DOMAIN 1..278
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 284 AA; 31287 MW; 2B06304508C3057A CRC64;
MKILVLGASG MLGSAVMRVL SEKKDWQLFG TVRSANAGRF FSPQIAECLL PGCDVENHDA
LVKVFDRVKP TVVINCIGLV KQLADADDPL LALPINSLLP HRLAALCNLS GARLIHISTD
CVFKGDKGAY EEKDISDATD LYGKSKFLGE VSLPQTLTLR TSIIGHELQN AHGLVEWFLE
QKDRCNGYKR SIFSGLPTVA LAQFIRDVVI PRADLSGLYH VAAKPISKFD LLALIADVYG
KEINILADES VVINRSLSAE KLRQDTGYEA PDWRSLIQLM HLYK
//