EPSD_RALSO
ID EPSD_RALSO Reviewed; 423 AA.
AC P58591;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=NDP-N-acetyl-D-galactosaminuronic acid dehydrogenase;
DE EC=1.1.1.-;
GN Name=epsD; OrderedLocusNames=RSp1016; ORFNames=RS02350;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG Plasmid megaplasmid Rsp.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
CC -!- FUNCTION: Probably involved in the synthesis of sugar components of EPS
CC I, by converting NDP-N-acetyl-D-galactosamine into NDP-N-acetyl-D-
CC galactosaminuronic acid. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AL646053; CAD18167.1; -; Genomic_DNA.
DR RefSeq; WP_011004306.1; NC_003296.1.
DR AlphaFoldDB; P58591; -.
DR SMR; P58591; -.
DR STRING; 267608.RSp1016; -.
DR EnsemblBacteria; CAD18167; CAD18167; RSp1016.
DR GeneID; 60503927; -.
DR KEGG; rso:RSp1016; -.
DR eggNOG; COG0677; Bacteria.
DR HOGENOM; CLU_023810_3_2_4; -.
DR OMA; IELANTH; -.
DR Proteomes; UP000001436; Plasmid megaplasmid Rsp.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR017476; UDP-Glc/GDP-Man.
DR InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
DR InterPro; IPR036220; UDP-Glc/GDP-Man_DH_C_sf.
DR InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer.
DR InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N.
DR InterPro; IPR028359; UDP_ManNAc/GlcNAc_DH.
DR Pfam; PF00984; UDPG_MGDP_dh; 1.
DR Pfam; PF03720; UDPG_MGDP_dh_C; 1.
DR Pfam; PF03721; UDPG_MGDP_dh_N; 1.
DR PIRSF; PIRSF500136; UDP_ManNAc_DH; 1.
DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR SMART; SM00984; UDPG_MGDP_dh_C; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52413; SSF52413; 1.
DR TIGRFAMs; TIGR03026; NDP-sugDHase; 1.
PE 3: Inferred from homology;
KW Lipopolysaccharide biosynthesis; NAD; Oxidoreductase; Plasmid;
KW Reference proteome.
FT CHAIN 1..423
FT /note="NDP-N-acetyl-D-galactosaminuronic acid
FT dehydrogenase"
FT /id="PRO_0000074073"
FT ACT_SITE 218
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT ACT_SITE 272
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT BINDING 11..28
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 423 AA; 46673 MW; 14A719FF9D822FDB CRC64;
MDRAIDIDFR TISVVGLGYI GLPTATVLAS RQREVIGVDI NQHAVDTINQ GRIHIVEPDL
DMLVRAAVSQ GYLRATTEPE PADAFLIAVP TPFLDNKQPD LSYIEAAARA IAPVLKRGDL
VVLESTSPVG ATEQLSDWLS AQRPDLSFPH QQGEESDIRV AHCPERVLPG HVLRELVEND
RIIGGMTPKC SEAAQRLYEL FVRGRCIVTD ARTAEMCKLT ENAFRDVNIA FANELSMICD
EIGVNVWELI SVANRHPRVN ILQPGPGVGG HCIAVDPWFI VDAAPESARL IRTAREVNDA
KPHYVLDRVK QAARRFKEPV IACFGLSFKA NIDDLRESPA IEIVQTMVQQ QLGTVLVVEP
HIKVLPAALQ GVELLNAEAA LSRADIVVLL VDHQQFRKLD TDRLQSRVVI DTRGMWSAKR
IAA