EPSD_RALSL
ID EPSD_RALSL Reviewed; 423 AA.
AC Q45410;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=NDP-N-acetyl-D-galactosaminuronic acid dehydrogenase;
DE EC=1.1.1.-;
GN Name=epsD;
OS Ralstonia solanacearum (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=305;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AW;
RX PubMed=7476194; DOI=10.1111/j.1365-2958.1995.tb02323.x;
RA Huang J., Schell M.;
RT "Molecular characterization of the eps gene cluster of Pseudomonas
RT solanacearum and its transcriptional regulation at a single promoter.";
RL Mol. Microbiol. 16:977-989(1995).
CC -!- FUNCTION: Probably involved in synthesis of sugar components of EPS I,
CC by converting NDP-N-acetyl-D-galactosamine into NDP-N-acetyl-D-
CC galactosaminuronic acid.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U17898; AAA91627.1; -; Genomic_DNA.
DR PIR; S77638; S77638.
DR AlphaFoldDB; Q45410; -.
DR SMR; Q45410; -.
DR STRING; 859657.RPSI07_mp1010; -.
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.
FT CHAIN 1..423
FT /note="NDP-N-acetyl-D-galactosaminuronic acid
FT dehydrogenase"
FT /id="PRO_0000074074"
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; 46803 MW; 405E93D11A09B13A CRC64;
MDRAIEIDFR TISVVGLGYI GLPTATVLAS RQRELIGVDI NQHAVDTINQ ARIHIVEPDL
DMLVRAAVSQ GYLRATTEPE PADAFLIAVP TPFLEDKQPD LTYIEAAAKA IAPVLKRGDL
VVLESTSPVG ATEQLSAWLS EQRSDLSFPH QLGEESDIRV AHCPERVLPG HVLRELVEND
RIIGGMTPRC SQAAQRLYEL FVRGRCIVTD ARTAEMCKLT ENAFRDVNIA FANELSMICD
EIGVNVWELI SVANRHPRVN ILQPGPGVGG HCIAVDPWFI VDAAPESARL IRTAREVNDA
KPHYVLDRVK QAARRFKEPV IACFGLSFKA NIDDLRESPA IEIVRTMVQQ QLGTVLVVEP
HIKVLPASLE GVELLNAEPA LSRADIVVLL VDHQKFRKLD TDRLQSRVVI DTRGMWSAKR
LAA