WECC_ECO57
ID WECC_ECO57 Reviewed; 420 AA.
AC P67066; Q8XAR7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=UDP-N-acetyl-D-mannosamine dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02029};
DE EC=1.1.1.336 {ECO:0000255|HAMAP-Rule:MF_02029};
DE AltName: Full=UDP-ManNAc 6-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02029};
GN Name=wecC {ECO:0000255|HAMAP-Rule:MF_02029}; Synonyms=rffD;
GN OrderedLocusNames=Z5298, ECs4720;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Catalyzes the four-electron oxidation of UDP-N-acetyl-D-
CC mannosamine (UDP-ManNAc), reducing NAD(+) and releasing UDP-N-
CC acetylmannosaminuronic acid (UDP-ManNAcA). {ECO:0000255|HAMAP-
CC Rule:MF_02029}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + 2 NAD(+) + UDP-N-acetyl-alpha-D-mannosamine = 3 H(+) + 2
CC NADH + UDP-N-acetyl-alpha-D-mannosaminouronate; Xref=Rhea:RHEA:25780,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:68623, ChEBI:CHEBI:70731;
CC EC=1.1.1.336; Evidence={ECO:0000255|HAMAP-Rule:MF_02029};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02029}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02029}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. WecC subfamily. {ECO:0000255|HAMAP-Rule:MF_02029}.
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DR EMBL; AE005174; AAG58982.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38143.1; -; Genomic_DNA.
DR PIR; B86065; B86065.
DR PIR; H91218; H91218.
DR RefSeq; NP_312747.1; NC_002695.1.
DR RefSeq; WP_000006621.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P67066; -.
DR SMR; P67066; -.
DR STRING; 155864.EDL933_5107; -.
DR EnsemblBacteria; AAG58982; AAG58982; Z5298.
DR EnsemblBacteria; BAB38143; BAB38143; ECs_4720.
DR GeneID; 66672310; -.
DR GeneID; 915235; -.
DR KEGG; ece:Z5298; -.
DR KEGG; ecs:ECs_4720; -.
DR PATRIC; fig|386585.9.peg.4924; -.
DR eggNOG; COG0677; Bacteria.
DR HOGENOM; CLU_023810_3_2_6; -.
DR OMA; IELANTH; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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:0089714; F:UDP-N-acetyl-D-mannosamine dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02029; WecC_RffD; 1.
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 InterPro; IPR032891; WecC.
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 NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..420
FT /note="UDP-N-acetyl-D-mannosamine dehydrogenase"
FT /id="PRO_0000074078"
FT ACT_SITE 212
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02029"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02029"
FT BINDING 10..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02029"
FT BINDING 160..161
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02029"
FT BINDING 212
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02029"
FT BINDING 216..219
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02029"
FT BINDING 250..252
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02029"
FT BINDING 263
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02029"
FT BINDING 330..331
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02029"
SQ SEQUENCE 420 AA; 45839 MW; DDD63F572FDEA463 CRC64;
MSFATISVIG LGYIGLPTAA AFASRQKQVI GVDINQHAVD TINRGEIHIV EPDLASVVKT
AVEGGFLRAS TTPVEADAWL IAVPTPFKGD HEPDMTYVES AARSIAPVLK KGALVILEST
SPVGSTEKMA EWLAEMRPDL TFPQQVGEQA DVNIAYCPER VLPGQVMVEL IKNDRVIGGM
TPVCSARASE LYKIFLEGEC VVTNSRTAEM CKLTENSFRD VNIAFANELS LICADQGINV
WELIRLANRH PRVNILQPGP GVGGHCIAVD PWFIVAQNPQ QARLIRTARE VNDHKPFWVI
DQVKAAVADC LAATDKRASE LKIACFGLAF KPNIDDLRES PAMEIAELIA QWHSGETLVV
EPNIHQLPKK LTGLCTLAQL DEALATADVL VMLVDHSQFK VINGDNVHQQ YVVDAKGVWR
