WECC_METJA
ID WECC_METJA Reviewed; 427 AA.
AC Q57871;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=MJ0428;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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; L77117; AAB98413.1; -; Genomic_DNA.
DR PIR; D64353; D64353.
DR RefSeq; WP_010869927.1; NC_000909.1.
DR AlphaFoldDB; Q57871; -.
DR SMR; Q57871; -.
DR STRING; 243232.MJ_0428; -.
DR EnsemblBacteria; AAB98413; AAB98413; MJ_0428.
DR GeneID; 1451288; -.
DR KEGG; mja:MJ_0428; -.
DR eggNOG; arCOG00252; Archaea.
DR HOGENOM; CLU_023810_3_2_2; -.
DR InParanoid; Q57871; -.
DR OMA; GHCLPID; -.
DR OrthoDB; 41144at2157; -.
DR PhylomeDB; Q57871; -.
DR Proteomes; UP000000805; 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..427
FT /note="UDP-N-acetyl-D-mannosamine dehydrogenase"
FT /id="PRO_0000074083"
FT REGION 157..158
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT REGION 213..216
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT REGION 247..249
FT /note="Substrate; shared with dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT REGION 317..318
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT ACT_SITE 209
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT ACT_SITE 263
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT BINDING 12..29
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O59284"
SQ SEQUENCE 427 AA; 47749 MW; 0F0EAAFC17F8BB76 CRC64;
MTKVEKNGIG KRICVIGLGY IGLPTASMLA IQGFDVIGVD INEKRVKEIK ELSFKTTEKD
LMTLVKGAIN SGNLKVQTKP EKADVFIICV PTPCIECDGE KKCDLTYLNK AIESIKPYLE
NGNLIIIEST IPPGTTDDIY KKLSKDKKIY VAHCPERVLP GSILKELVEN DRVIGGVDEK
SAEMAKEIYE TFVTGKIYLT DAKTAEMVKL MENTYRDVNI ALANEFAKIA EEIGINVWEA
IELANKHPRV NILKPGPGVG GHCISIDPWF IVEKSKNAKL IRTARELNDS MPLFVVEKIK
KIIKKDIGKV AIFGVTYKGN VDDTRESPAE KVVSKLIDEG FEVKCYDKYA RDFIYPLNSL
DEAVEGADII VILAEHDEYK NFDKEDIKNI ASKVKNKIIL DTKNILNREL WEKEGFKVYV
LGDGKNA
