WECC_SALTY
ID WECC_SALTY Reviewed; 420 AA.
AC Q9L6R4;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, 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=STM3921; ORFNames=STMD1.69;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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; AE006468; AAL22770.1; -; Genomic_DNA.
DR EMBL; AF233324; AAF33466.1; -; Genomic_DNA.
DR RefSeq; NP_462811.1; NC_003197.2.
DR RefSeq; WP_000011227.1; NC_003197.2.
DR AlphaFoldDB; Q9L6R4; -.
DR SMR; Q9L6R4; -.
DR STRING; 99287.STM3921; -.
DR PaxDb; Q9L6R4; -.
DR EnsemblBacteria; AAL22770; AAL22770; STM3921.
DR GeneID; 1255447; -.
DR KEGG; stm:STM3921; -.
DR PATRIC; fig|99287.12.peg.4142; -.
DR HOGENOM; CLU_023810_3_2_6; -.
DR OMA; IELANTH; -.
DR PhylomeDB; Q9L6R4; -.
DR BioCyc; SENT99287:STM3921-MON; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000001014; 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_0000074080"
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; 45339 MW; 87F9274F9C8F4EEC CRC64;
MSFTTISVIG LGYIGLPTAA AFASRQKQVI GVDINQHAVD IINRGEIHIV EPALGNVVKM
AVEGGFLRAT TTPVEADAYL IAVPTPFKGD HDPDMAYVEA AAKSIAPVLK KGALVILEST
SPVGATEQMA GWLAGMRTDL TFPQQAGEQA DVNIAYCPER VLPGQVMVEL IKNDRVIGGM
TPVCSARASA LYKIFLEGEC VVTNSRTAEM CKLTENSFRD VNIAFANELS LICAEQGINV
WELIRLANRH PRVNILQPGP GVGGHCIAVD PWFIVAQNPQ QARLIRTARE VNDGKPHWVV
DQVKAAVTDC LAATDKRASE VKIACFGLAF KPNIDDLRES PAMGIAQSIA RWHSGETLVV
EPNIRQLPKK LDGLCTLAKL DAALAAADVL VMLVDHDEFK AIPGDAVHQR YVVDTKGVWR
