ID   WECC_METVS              Reviewed;         427 AA.
AC   A6USK4;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Mevan_1584;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS   / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
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., Anderson I.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
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; CP000742; ABR55476.1; -; Genomic_DNA.
DR   RefSeq; WP_012066390.1; NC_009634.1.
DR   AlphaFoldDB; A6USK4; -.
DR   SMR; A6USK4; -.
DR   STRING; 406327.Mevan_1584; -.
DR   EnsemblBacteria; ABR55476; ABR55476; Mevan_1584.
DR   GeneID; 5324798; -.
DR   KEGG; mvn:Mevan_1584; -.
DR   eggNOG; arCOG00252; Archaea.
DR   HOGENOM; CLU_023810_3_2_2; -.
DR   OMA; GHCLPID; -.
DR   OrthoDB; 41144at2157; -.
DR   Proteomes; UP000001107; 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_0000337839"
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;  47791 MW;  7C0571F6664023F9 CRC64;
     MDKHEKQKIK KICVIGLGYI GLPTASMLAN HGYEVIGVDI SEKRVNEIKN GDFKIEEPGL
     LTLLKGAINS KNLNVKTKAE KADAFIICVP TPAIGCDDGS KKCDLSYVLD AVNSILPYID
     EGNLIVIEST IPPETTQKIY DIIDKKVYVA HCPERVLPGK ILKELVENDR IIGGINKKSA
     EMAKEIYKSF VEGKIYITDS NTAEMVKLME NTYRDINIAL ANEFAKICDE IGVNVWDAIK
     IANKHPRVNI LNPGPGVGGH CISIDPWFIV EKTNNAKFIR SARELNDKMP YYVCNMIISE
     LKNLNIEKPK VTVFGATYKG NVEDTRESPS KKVIDALAEK NIPVSTYDPH ANSFEYELHS
     LEDSIVNSDC IVVLTDHNEF KSFKKEEIDE ISKKLKNKLI IDTKNILNHN LWKKAGFKIK
     LLGNGAW