ID   WECC_META3              Reviewed;         438 AA.
AC   A6UU98;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=UDP-N-acetyl-D-mannosamine dehydrogenase;
DE            EC=1.1.1.336 {ECO:0000250|UniProtKB:Q6LZC3};
DE   AltName: Full=UDP-ManNAc 6-dehydrogenase;
GN   Name=wecC; OrderedLocusNames=Maeo_0484;
OS   Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS   Nankai-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=419665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus aeolicus Nankai-3.";
RL   Submitted (JUN-2007) 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).
CC       {ECO:0000250|UniProtKB:Q6LZC3}.
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:0000250|UniProtKB:Q6LZC3};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q6LZC3}.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; CP000743; ABR56070.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6UU98; -.
DR   SMR; A6UU98; -.
DR   STRING; 419665.Maeo_0484; -.
DR   EnsemblBacteria; ABR56070; ABR56070; Maeo_0484.
DR   KEGG; mae:Maeo_0484; -.
DR   eggNOG; arCOG00252; Archaea.
DR   HOGENOM; CLU_023810_3_2_2; -.
DR   OMA; GHCLPID; -.
DR   Proteomes; UP000001106; 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-EC.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
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   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..438
FT                   /note="UDP-N-acetyl-D-mannosamine dehydrogenase"
FT                   /id="PRO_0000337835"
FT   REGION          160..161
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O59284"
FT   REGION          216..219
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O59284"
FT   REGION          250..252
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000250|UniProtKB:O59284"
FT   REGION          323..324
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O59284"
FT   ACT_SITE        212
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O59284"
FT   ACT_SITE        266
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O59284"
FT   BINDING         13..30
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O59284"
FT   BINDING         263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O59284"
SQ   SEQUENCE   438 AA;  48982 MW;  4920818595610317 CRC64;
     MKLDKSKQKE INKICVVGLG YIGLPTASML AIQGYKVIGV DIDEERVKTI RDGKLIINEQ
     GLMTLLTGAI TSGNLVVKTE PEEADVYIIC VPTPATADKN GKKCDLICVL SAVNNIKPYL
     KDGDLIIIES TIPPKTTEKI YDDISKNTGK NIYMAYCPER VLPGNILKEL VENDRTIGGI
     NKKSAQLAKE IYASFIEGNL YITDSTTAEM VKLMENTFRD VNIALANEFA KVSTELDINV
     WDAINLANKH PRVNILNPGP GVGGHCISID PWFIVGSSEN AELIKKARNL NDDMPKYVAS
     LIIKEFKEMG ICNPKVGIFG ITYKGDVEDT RETPARAIID YLLQNDFEVS IYDPYAKDFE
     YPLNTIEESI KNSDALIFLT DHSEFKNFEK EDIKEISHMM KNKIVMDMKN TLNHNLWEEQ
     GFNVKLLGDG KSWIVKTL