ID W0LDF9_9GAMM Unreviewed; 420 AA.
AC W0LDF9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
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 ECO:0000313|EMBL:AHG20414.1};
GN ORFNames=Z042_12815 {ECO:0000313|EMBL:AHG20414.1};
OS Chania multitudinisentens RB-25.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Chania.
OX NCBI_TaxID=1441930 {ECO:0000313|EMBL:AHG20414.1, ECO:0000313|Proteomes:UP000019030};
RN [1] {ECO:0000313|EMBL:AHG20414.1, ECO:0000313|Proteomes:UP000019030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RB-25 {ECO:0000313|EMBL:AHG20414.1,
RC ECO:0000313|Proteomes:UP000019030};
RA Robson E.H.J.;
RT "Isolation of Serratia multitudinisentens RB-25 from Ex-Landfill site.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AHG20414.1, ECO:0000313|Proteomes:UP000019030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RB-25 {ECO:0000313|EMBL:AHG20414.1,
RC ECO:0000313|Proteomes:UP000019030};
RA Chan K.-G.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP007044; AHG20414.1; -; Genomic_DNA.
DR RefSeq; WP_024912372.1; NZ_JAJC01000014.1.
DR AlphaFoldDB; W0LDF9; -.
DR STRING; 1441930.Z042_12815; -.
DR KEGG; sfo:Z042_12815; -.
DR PATRIC; fig|1441930.4.peg.2547; -.
DR eggNOG; COG0677; Bacteria.
DR HOGENOM; CLU_023810_3_2_6; -.
DR OrthoDB; 9803238at2; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000019030; 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}; Reference proteome {ECO:0000313|Proteomes:UP000019030}.
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; 45732 MW; 654D2DF3EC10E009 CRC64;
MSFNTISVIG LGYIGLPTAA AFASRKKKVV GVDVNQHAVD TINRGAIHIV EPDLDRVVKE
AVEGGYLQAV SKPLAADAFL IAVPTPFKGD HEPDLAYVEA AARSLAPVLK KGDLVILEST
SPVGATEQMA QWLAEARSDL SFPQNAGEQA DVNIAYCPER VLPGQVMVEL IRNDRVIGGM
TPKCSERASA LYKIFLEGEC VVTNSRTAEM CKLTENSFRD VNIAFANELS LICAEQGINV
WELIRLANRH PRVNILQPGP GVGGHCIAVD PWFIVAQNPQ QARLIHTARL VNDGKPLWVV
DRVKTAVADC LAATNKRASE VKIACFGLAF KPNIDDLRES PAVEVAHLIA DWHVGETLAV
EPNVEQLPKS LAGHVILKDL AVALHQADVI VMLVDHKEFK AIKPEEIKQT WIVDTKGVWR
//
