ID   WECC_METM5              Reviewed;         427 AA.
AC   A4FY94;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-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=MmarC5_0870;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
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., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-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}.
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; CP000609; ABO35178.1; -; Genomic_DNA.
DR   RefSeq; WP_011868632.1; NC_009135.1.
DR   AlphaFoldDB; A4FY94; -.
DR   SMR; A4FY94; -.
DR   STRING; 402880.MmarC5_0870; -.
DR   EnsemblBacteria; ABO35178; ABO35178; MmarC5_0870.
DR   GeneID; 4928426; -.
DR   KEGG; mmq:MmarC5_0870; -.
DR   eggNOG; arCOG00252; Archaea.
DR   HOGENOM; CLU_023810_3_2_2; -.
DR   OMA; GHCLPID; -.
DR   OrthoDB; 41144at2157; -.
DR   Proteomes; UP000000253; 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.
FT   CHAIN           1..427
FT                   /note="UDP-N-acetyl-D-mannosamine dehydrogenase"
FT                   /id="PRO_0000337837"
FT   REGION          155..156
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O59284"
FT   REGION          211..214
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O59284"
FT   REGION          245..247
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000250|UniProtKB:O59284"
FT   REGION          318..319
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O59284"
FT   ACT_SITE        207
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O59284"
FT   ACT_SITE        261
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O59284"
FT   BINDING         11..28
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O59284"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O59284"
SQ   SEQUENCE   427 AA;  47374 MW;  EC019825C3816394 CRC64;
     MEKHGNYNIN KICVIGLGYI GLPTASMLAN HGYEVVGVDV NEKRVNQIKN GELKIEEPGL
     LTLVKGAINS KNLNVQTSAT EADAFIICVP TPALENEDGS KKCDLTYVMG AVQNIIPFLK
     EGNLIVIEST IPPEITKKIY ETIDKKIYVA HCPERVLPGK ILKELVENDR IIGGINKKSA
     EMAKEIYKSF VEGKIYITDS NTAEMVKLME NTYRDINIAL ANEFAKICDE IGVNVWDAIK
     IANKHPRVNI LNPGPGVGGH CISIDPWFIV EKTNNAKFIR AARELNDNMP AYVCKSVLSE
     LKKHGIKKPK ISVFGATYKG NVEDTRESPS KNVIEMLLKN GVTVSTFDPH ATCFEYPLST
     LDECISGSDC IVVLTDHDAF KNIKKDDIDE ICPKLKNKIV FDTKNILEHN LWKRAGFTVK
     LLGNGAW