WECC_SHIFL
ID WECC_SHIFL Reviewed; 420 AA.
AC P67067; Q8XAR7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=SF3861, S3899;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN45298.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18900.1; -; Genomic_DNA.
DR RefSeq; NP_709591.1; NC_004337.2.
DR RefSeq; WP_000006621.1; NZ_WPGW01000028.1.
DR AlphaFoldDB; P67067; -.
DR SMR; P67067; -.
DR STRING; 198214.SF3861; -.
DR EnsemblBacteria; AAN45298; AAN45298; SF3861.
DR EnsemblBacteria; AAP18900; AAP18900; S3899.
DR GeneID; 1026028; -.
DR GeneID; 66672310; -.
DR KEGG; sfl:SF3861; -.
DR KEGG; sfx:S3899; -.
DR PATRIC; fig|198214.7.peg.4551; -.
DR HOGENOM; CLU_023810_3_2_6; -.
DR OMA; IELANTH; -.
DR OrthoDB; 295459at2; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000074081"
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
