ID C5BBB8_EDWI9 Unreviewed; 420 AA.
AC C5BBB8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=UDP-N-acetyl-D-mannosamine dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02029};
DE EC=1.1.1.336 {ECO:0000256|HAMAP-Rule:MF_02029};
DE AltName: Full=UDP-ManNAc 6-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02029};
GN Name=wecC {ECO:0000256|HAMAP-Rule:MF_02029};
GN OrderedLocusNames=NT01EI_0093 {ECO:0000313|EMBL:ACR67353.1};
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67353.1, ECO:0000313|Proteomes:UP000001485};
RN [1] {ECO:0000313|Proteomes:UP000001485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACR67353.1, ECO:0000313|Proteomes:UP000001485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146 {ECO:0000313|EMBL:ACR67353.1,
RC ECO:0000313|Proteomes:UP000001485};
RX PubMed=22247535; DOI=10.1128/JB.06522-11;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA Lawrence M.L.;
RT "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated with
RT a Natural Channel Catfish Outbreak of Enteric Septicemia of Catfish.";
RL J. Bacteriol. 194:740-741(2012).
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:0000256|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:0000256|HAMAP-Rule:MF_02029};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02029}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02029}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. WecC subfamily. {ECO:0000256|HAMAP-Rule:MF_02029}.
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; CP001600; ACR67353.1; -; Genomic_DNA.
DR RefSeq; WP_015869572.1; NC_012779.2.
DR AlphaFoldDB; C5BBB8; -.
DR STRING; 67780.B6E78_11625; -.
DR GeneID; 69537202; -.
DR KEGG; eic:NT01EI_0093; -.
DR PATRIC; fig|634503.3.peg.87; -.
DR HOGENOM; CLU_023810_3_2_6; -.
DR OrthoDB; 9803238at2; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000001485; 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 Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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 NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR PANTHER; PTHR43491; UDP-N-ACETYL-D-MANNOSAMINE DEHYDROGENASE; 1.
DR PANTHER; PTHR43491:SF1; UDP-N-ACETYL-D-MANNOSAMINE DEHYDROGENASE; 1.
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; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52413; UDP-glucose/GDP-mannose dehydrogenase C-terminal domain; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_02029};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02029}.
FT DOMAIN 324..420
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT ACT_SITE 212
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 160
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 161
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 212
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 216
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 219
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 250
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 252
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 263
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 330
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 331
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 338
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 416
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
SQ SEQUENCE 420 AA; 45745 MW; 870B3BCF7790A0C4 CRC64;
MSFDTISVIG LGYIGLPTAV AFAGCRKQVI GVDVSQHAVE TINRGEIHIV EPDLDRAVKR
AVEGGFLRAV MRPEPADAFL IAVPTPFKGE HEPDLTYVEA AARSIAPVLK KGDLVILEST
SPVGATEQMC AWLAECRADL RFPHQDGEQA DIRVAYCPER VLPGKIMVEL LRNDRVIGGM
TPTCSAQASA LYRLFLEGEC VETNARTAEM CKLTENSFRD VNIAFANELS LICDAQGIDV
WQLIALANRH PRVNILQPGP GVGGHCIAVD PWFIVAQNPQ LARLIHTARL VNDGKPLWVV
DRVKAALADC LAAEDKRASE ATIACFGLAF KPDIDDLRES PAMEITEMVA QWHSGTTLVV
EPNIHQLPVR LAGMAQLTDC TTALAQADVV VLLVDHQPFR ALAPQAVTQR FVVDTKGVWR
//
