RMD_PSEAE
ID RMD_PSEAE Reviewed; 304 AA.
AC Q9HTB6; O87265;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=GDP-6-deoxy-D-mannose reductase;
DE EC=1.1.1.281;
GN Name=rmd; OrderedLocusNames=PA5454;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9781879; DOI=10.1046/j.1365-2958.1998.01024.x;
RA Rocchetta H.L., Pacan J.C., Lam J.S.;
RT "Synthesis of the A-band polysaccharide sugar D-rhamnose requires Rmd and
RT WbpW: identification of multiple AlgA homologues, WbpW and ORF488, in
RT Pseudomonas aeruginosa.";
RL Mol. Microbiol. 29:1419-1434(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11856318; DOI=10.1046/j.0014-2956.2001.02688.x;
RA Maeki M., Jaervinen N., Raebinae J., Roos C., Maaheimo H., Renkonen R.;
RT "Functional expression of Pseudomonas aeruginosa GDP-4-keto-6-deoxy-D-
RT mannose reductase which synthesizes GDP-rhamnose.";
RL Eur. J. Biochem. 269:593-601(2002).
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:11856318, ECO:0000269|PubMed:9781879}.
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:11856318, ECO:0000269|PubMed:9781879};
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:11856318, ECO:0000269|PubMed:9781879};
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. GDP-6-deoxy-D-mannose reductase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72282.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF009955; AAC72282.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE004091; AAG08839.1; -; Genomic_DNA.
DR PIR; H82964; H82964.
DR RefSeq; NP_254141.1; NC_002516.2.
DR RefSeq; WP_003114107.1; NZ_QZGE01000012.1.
DR PDB; 6X3B; X-ray; 1.91 A; A/B/C/D=1-304.
DR PDBsum; 6X3B; -.
DR AlphaFoldDB; Q9HTB6; -.
DR SMR; Q9HTB6; -.
DR STRING; 287.DR97_2833; -.
DR PaxDb; Q9HTB6; -.
DR PRIDE; Q9HTB6; -.
DR EnsemblBacteria; AAG08839; AAG08839; PA5454.
DR GeneID; 883037; -.
DR KEGG; pae:PA5454; -.
DR PATRIC; fig|208964.12.peg.5717; -.
DR PseudoCAP; PA5454; -.
DR HOGENOM; CLU_007383_1_7_6; -.
DR InParanoid; Q9HTB6; -.
DR OMA; RLRPFNH; -.
DR PhylomeDB; Q9HTB6; -.
DR BioCyc; PAER208964:G1FZ6-5582-MON; -.
DR BRENDA; 1.1.1.281; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0033705; F:GDP-4-dehydro-6-deoxy-D-mannose reductase activity; IDA:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; EXP:PseudoCAP.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0019306; P:GDP-D-rhamnose biosynthetic process; EXP:PseudoCAP.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IMP:PseudoCAP.
DR GO; GO:0009243; P:O antigen biosynthetic process; IDA:PseudoCAP.
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; Reference proteome.
FT CHAIN 1..304
FT /note="GDP-6-deoxy-D-mannose reductase"
FT /id="PRO_0000419038"
FT BINDING 13..14
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 39..40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 105..106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 260..263
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:6X3B"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:6X3B"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:6X3B"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:6X3B"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:6X3B"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:6X3B"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:6X3B"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:6X3B"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:6X3B"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:6X3B"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:6X3B"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:6X3B"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6X3B"
FT HELIX 130..149
FT /evidence="ECO:0007829|PDB:6X3B"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:6X3B"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6X3B"
FT HELIX 171..183
FT /evidence="ECO:0007829|PDB:6X3B"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:6X3B"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:6X3B"
FT HELIX 205..218
FT /evidence="ECO:0007829|PDB:6X3B"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:6X3B"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:6X3B"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:6X3B"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:6X3B"
FT HELIX 272..278
FT /evidence="ECO:0007829|PDB:6X3B"
FT HELIX 286..300
FT /evidence="ECO:0007829|PDB:6X3B"
SQ SEQUENCE 304 AA; 33929 MW; 4A0DB2CFB49A1000 CRC64;
MTQRLFVTGL SGFVGKHLQA YLAAAHTPWA LLPVPHRYDL LEPDSLGDLW PELPDAVIHL
AGQTYVPEAF RDPARTLQIN LLGTLNLLQA LKARGFSGTF LYISSGDVYG QVAEAALPIH
EELIPHPRNP YAVSKLAAES LCLQWGITEG WRVLVARPFN HIGPGQKDSF VIASAARQIA
RMKQGLQANR LEVGDIDVSR DFLDVQDVLS AYLRLLSHGE AGAVYNVCSG QEQKIRELIE
LLADIAQVEL EIVQDPARMR RAEQRRVRGS HARLHDTTGW KPEITIKQSL RAILSDWESR
VREE
