ID   WECC_METM7              Reviewed;         427 AA.
AC   A6VK13;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=MmarC7_1733;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
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; CP000745; ABR66789.1; -; Genomic_DNA.
DR   RefSeq; WP_012068249.1; NC_009637.1.
DR   AlphaFoldDB; A6VK13; -.
DR   SMR; A6VK13; -.
DR   STRING; 426368.MmarC7_1733; -.
DR   EnsemblBacteria; ABR66789; ABR66789; MmarC7_1733.
DR   GeneID; 5328535; -.
DR   KEGG; mmz:MmarC7_1733; -.
DR   eggNOG; arCOG00252; Archaea.
DR   HOGENOM; CLU_023810_3_2_2; -.
DR   OMA; GHCLPID; -.
DR   OrthoDB; 41144at2157; -.
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_0000337838"
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;  47334 MW;  24EC219F25D7C307 CRC64;
     MEKHGNYDIK KICVIGLGYI GLPTASMLAN HGYEVVGVDV NEKRVNHIKN GELKIEEPGL
     LTLVKGAINS KNLNVQTSAE EADAFIICVP TPALENEDGS KKCDLTYVMS AVQAIIPFLK
     DGNLIVVEST IPPETTKKIY ETINKKIYVA HCPERVLPGK ILKELVENDR IIGGINKKSA
     EMAKEIYKSF VEGKIYITDS NTAEMVKLME NTYRDINIAL ANEFAKICDE IGVNVWDAIK
     IANKHPRVNI LNPGPGVGGH CISIDPWFIV EKTNNAKFIR AARELNDNMP AYVCKSVLSE
     LNKLGIEKPK ISIFGATYKG NVEDTRESPS KNVIKMLLEN GATVSTFDPH ADCFEYPLST
     LDECISGSDC IVVLTDHDAF KNIKKDDIDE ICPKLKNKIV FDTKNILEHN LWKKAGFKVK
     LLGNGAW