RMD_ANETH
ID RMD_ANETH Reviewed; 309 AA.
AC Q6T1X6;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=GDP-6-deoxy-D-mannose reductase;
DE EC=1.1.1.281;
GN Name=rmd;
OS Aneurinibacillus thermoaerophilus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=143495;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=L420-91T;
RX PubMed=11096116; DOI=10.1074/jbc.m010027200;
RA Kneidinger B., Graninger M., Adam G., Puchberger M., Kosma P., Zayni S.,
RA Messner P.;
RT "Identification of two GDP-6-deoxy-D-lyxo-4-hexulose reductases
RT synthesizing GDP-D-rhamnose in Aneurinibacillus thermoaerophilus L420-
RT 91T.";
RL J. Biol. Chem. 276:5577-5583(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND NADP
RP ANALOG, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19459932; DOI=10.1111/j.1742-4658.2009.06993.x;
RA King J.D., Poon K.K.H., Webb N.A., Anderson E.M., McNally D.J.,
RA Brisson J.-R., Messner P., Garavito R.M., Lam J.S.;
RT "The structural basis for catalytic function of GMD and RMD, two closely
RT related enzymes from the GDP-D-rhamnose biosynthesis pathway.";
RL FEBS J. 276:2686-2700(2009).
CC -!- FUNCTION: Reductase that catalyzes the conversion of GDP-6-deoxy-D-
CC mannose to GDP-4-dehydro-6-deoxy-D-mannose (GDP-D-rhamnose).
CC {ECO:0000269|PubMed:11096116, ECO:0000269|PubMed:19459932}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-alpha-D-rhamnose + NAD(+) = GDP-4-dehydro-alpha-D-rhamnose
CC + H(+) + NADH; Xref=Rhea:RHEA:13825, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57964,
CC ChEBI:CHEBI:58224; EC=1.1.1.281;
CC Evidence={ECO:0000269|PubMed:11096116, ECO:0000269|PubMed:19459932};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-alpha-D-rhamnose + NADP(+) = GDP-4-dehydro-alpha-D-
CC rhamnose + H(+) + NADPH; Xref=Rhea:RHEA:13829, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57964, ChEBI:CHEBI:58224,
CC ChEBI:CHEBI:58349; EC=1.1.1.281;
CC Evidence={ECO:0000269|PubMed:11096116, ECO:0000269|PubMed:19459932};
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. GDP-6-deoxy-D-mannose reductase subfamily. {ECO:0000305}.
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DR EMBL; AY442352; AAS55712.1; -; Genomic_DNA.
DR RefSeq; WP_057897460.1; NZ_FNDE01000013.1.
DR PDB; 2PK3; X-ray; 1.82 A; A/B=1-309.
DR PDBsum; 2PK3; -.
DR AlphaFoldDB; Q6T1X6; -.
DR SMR; Q6T1X6; -.
DR KEGG; ag:AAS55712; -.
DR EvolutionaryTrace; Q6T1X6; -.
DR GO; GO:0033705; F:GDP-4-dehydro-6-deoxy-D-mannose reductase activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; NADP; Oxidoreductase.
FT CHAIN 1..309
FT /note="GDP-6-deoxy-D-mannose reductase"
FT /id="PRO_0000419037"
FT BINDING 11..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 32
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 47..48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 71..73
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 114..115
FT /ligand="substrate"
FT BINDING 140
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19459932"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19459932"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19459932"
FT BINDING 269..272
FT /ligand="substrate"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2PK3"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:2PK3"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:2PK3"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:2PK3"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:2PK3"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:2PK3"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:2PK3"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:2PK3"
FT HELIX 82..103
FT /evidence="ECO:0007829|PDB:2PK3"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:2PK3"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2PK3"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2PK3"
FT HELIX 139..158
FT /evidence="ECO:0007829|PDB:2PK3"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:2PK3"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:2PK3"
FT HELIX 180..192
FT /evidence="ECO:0007829|PDB:2PK3"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:2PK3"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:2PK3"
FT HELIX 214..227
FT /evidence="ECO:0007829|PDB:2PK3"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:2PK3"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2PK3"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:2PK3"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:2PK3"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:2PK3"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:2PK3"
FT HELIX 281..287
FT /evidence="ECO:0007829|PDB:2PK3"
FT HELIX 295..307
FT /evidence="ECO:0007829|PDB:2PK3"
SQ SEQUENCE 309 AA; 34556 MW; 737FFC9390B14868 CRC64;
MRALITGVAG FVGKYLANHL TEQNVEVFGT SRNNEAKLPN VEMISLDIMD SQRVKKVISD
IKPDYIFHLA AKSSVKDSWL NKKGTFSTNV FGTLHVLDAV RDSNLDCRIL TIGSSEEYGM
ILPEESPVSE ENQLRPMSPY GVSKASVGML ARQYVKAYGM DIIHTRTFNH IGPGQSLGFV
TQDFAKQIVD IEMEKQEPII KVGNLEAVRD FTDVRDIVQA YWLLSQYGKT GDVYNVCSGI
GTRIQDVLDL LLAMANVKID TELNPLQLRP SEVPTLIGSN KRLKDSTGWK PRIPLEKSLF
EILQSYRQA
