WECC_ECOLI
ID WECC_ECOLI Reviewed; 420 AA.
AC P27829; Q2M895;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 4.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=UDP-N-acetyl-D-mannosamine dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02029, ECO:0000303|PubMed:381306};
DE EC=1.1.1.336 {ECO:0000255|HAMAP-Rule:MF_02029, ECO:0000269|PubMed:381306};
DE AltName: Full=UDP-ManNAc 6-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02029, ECO:0000305};
GN Name=wecC {ECO:0000255|HAMAP-Rule:MF_02029};
GN Synonyms=rffD {ECO:0000303|PubMed:2166030};
GN OrderedLocusNames=b3787, JW5599;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8226648; DOI=10.1128/jb.175.21.7074-7080.1993;
RA Kiino D.R., Licudine R., Wilt K., Yang D.H.C., Rothman-Denes L.B.;
RT "A cytoplasmic protein, NfrC, is required for bacteriophage N4
RT adsorption.";
RL J. Bacteriol. 175:7074-7080(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP SEQUENCE REVISION TO 78.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=014:K7:H-;
RX PubMed=381306; DOI=10.1016/s0021-9258(19)86913-2;
RA Kawamura T., Ishimoto N., Ito E.;
RT "Enzymatic synthesis of uridine diphosphate N-acetyl-D-mannosaminuronic
RT acid.";
RL J. Biol. Chem. 254:8457-8465(1979).
RN [7]
RP PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=2166030; DOI=10.1016/s0021-9258(18)77373-0;
RA Meier-Dieter U., Starman R., Barr K., Mayer H., Rick P.D.;
RT "Biosynthesis of enterobacterial common antigen in Escherichia coli.
RT Biochemical characterization of Tn10 insertion mutants defective in
RT enterobacterial common antigen synthesis.";
RL J. Biol. Chem. 265:13490-13497(1990).
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, ECO:0000269|PubMed:381306}.
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 ECO:0000269|PubMed:381306};
CC -!- ACTIVITY REGULATION: Activated by N-acetylglucosamine-1-P or K(+) at
CC low UDP-ManNAc concentrations. {ECO:0000269|PubMed:381306}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.22 mM for UDP-ManNAc (in the presence of 1 mM N-
CC acetylglucosamine-1-P) {ECO:0000269|PubMed:381306};
CC KM=0.11 mM for UDP-ManNAc (in the presence of 150 mM KCl)
CC {ECO:0000269|PubMed:381306};
CC KM=0.38 mM for UDP-ManNAc (in the absence of activators)
CC {ECO:0000269|PubMed:381306};
CC KM=0.21 mM for NAD(+) {ECO:0000269|PubMed:381306};
CC pH dependence:
CC Optimum pH is 10.0. {ECO:0000269|PubMed:381306};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02029,
CC ECO:0000269|PubMed:2166030}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:381306}.
CC -!- DISRUPTION PHENOTYPE: Mutants do not synthesize Und-PP-GlcNAc-ManNAcA
CC (lipid II) and enterobacterial common antigen (ECA).
CC {ECO:0000269|PubMed:2166030}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. WecC subfamily. {ECO:0000255|HAMAP-Rule:MF_02029, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA67587.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L18799; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; M87049; AAA67587.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAT48212.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77511.1; -; Genomic_DNA.
DR PIR; F65182; F65182.
DR RefSeq; WP_000006621.1; NZ_STEB01000021.1.
DR RefSeq; YP_026254.1; NC_000913.3.
DR AlphaFoldDB; P27829; -.
DR SMR; P27829; -.
DR BioGRID; 4262604; 229.
DR STRING; 511145.b3787; -.
DR jPOST; P27829; -.
DR PaxDb; P27829; -.
DR PRIDE; P27829; -.
DR EnsemblBacteria; AAT48212; AAT48212; b3787.
DR EnsemblBacteria; BAE77511; BAE77511; BAE77511.
DR GeneID; 66672310; -.
DR GeneID; 948977; -.
DR KEGG; ecj:JW5599; -.
DR KEGG; eco:b3787; -.
DR PATRIC; fig|1411691.4.peg.2919; -.
DR EchoBASE; EB1421; -.
DR eggNOG; COG0677; Bacteria.
DR HOGENOM; CLU_023810_3_2_6; -.
DR InParanoid; P27829; -.
DR OMA; IELANTH; -.
DR PhylomeDB; P27829; -.
DR BioCyc; EcoCyc:UDPMANNACADEHYDROG-MON; -.
DR BioCyc; MetaCyc:UDPMANNACADEHYDROG-MON; -.
DR SABIO-RK; P27829; -.
DR UniPathway; UPA00566; -.
DR PRO; PR:P27829; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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; IDA:EcoCyc.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..420
FT /note="UDP-N-acetyl-D-mannosamine dehydrogenase"
FT /id="PRO_0000074077"
FT ACT_SITE 212
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O59284, ECO:0000255|HAMAP-
FT Rule:MF_02029"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O59284, ECO:0000255|HAMAP-
FT Rule:MF_02029"
FT BINDING 10..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P11759, ECO:0000255|HAMAP-
FT 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:0000250|UniProtKB:O59284, ECO:0000255|HAMAP-
FT 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:0000250|UniProtKB:O59284, ECO:0000255|HAMAP-
FT 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:0000250|UniProtKB:O59284, ECO:0000255|HAMAP-
FT Rule:MF_02029"
FT BINDING 250..252
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:O59284, ECO:0000255|HAMAP-
FT 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:0000250|UniProtKB:O59284, ECO:0000255|HAMAP-
FT 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:0000250|UniProtKB:O59284, ECO:0000255|HAMAP-
FT Rule:MF_02029"
FT CONFLICT 78
FT /note="A -> R (in Ref. 2; AAA67587)"
FT /evidence="ECO:0000305"
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
