ID WECC_METMP Reviewed; 427 AA.
AC Q6LZC3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=UDP-N-acetyl-D-mannosamine dehydrogenase;
DE EC=1.1.1.336;
DE AltName: Full=UDP-ManNAc 6-dehydrogenase;
GN Name=wecC; OrderedLocusNames=MMP0706;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP AND SUBUNIT.
RC STRAIN=900;
RX PubMed=18263721; DOI=10.1128/jb.01970-07;
RA Namboori S.C., Graham D.E.;
RT "Acetamido sugar biosynthesis in the Euryarchaea.";
RL J. Bacteriol. 190:2987-2996(2008).
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). Cannot use NADP instead of
CC NAD. {ECO:0000269|PubMed:18263721}.
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:0000269|PubMed:18263721};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.57 mM for NAD(+) {ECO:0000269|PubMed:18263721};
CC -!- SUBUNIT: Homotetramer; probably dimer of dimers.
CC {ECO:0000269|PubMed:18263721}.
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; BX950229; CAF30262.1; -; Genomic_DNA.
DR RefSeq; WP_011170650.1; NC_005791.1.
DR AlphaFoldDB; Q6LZC3; -.
DR SMR; Q6LZC3; -.
DR STRING; 267377.MMP0706; -.
DR EnsemblBacteria; CAF30262; CAF30262; MMP0706.
DR GeneID; 2761881; -.
DR KEGG; mmp:MMP0706; -.
DR PATRIC; fig|267377.15.peg.723; -.
DR eggNOG; arCOG00252; Archaea.
DR HOGENOM; CLU_023810_3_2_2; -.
DR OrthoDB; 372050at2157; -.
DR BRENDA; 1.1.1.336; 3262.
DR SABIO-RK; Q6LZC3; -.
DR Proteomes; UP000000590; 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:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:CACAO.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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 NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR PANTHER; PTHR43491; UDP-N-ACETYL-D-MANNOSAMINE DEHYDROGENASE; 1.
DR PANTHER; PTHR43491:SF2; UDP-N-ACETYL-D-MANNOSAMINE DEHYDROGENASE; 1.
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; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52413; UDP-glucose/GDP-mannose dehydrogenase C-terminal domain; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..427
FT /note="UDP-N-acetyl-D-mannosamine dehydrogenase"
FT /id="PRO_0000337836"
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 19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 20
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 44
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 91
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 155
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT BINDING 156
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT BINDING 207
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT BINDING 211
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT BINDING 214
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT BINDING 245
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT BINDING 247
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT BINDING 258
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT BINDING 318
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT BINDING 319
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:O59284"
FT BINDING 326
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 404
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:O59284"
SQ SEQUENCE 427 AA; 47252 MW; 1B5780FBFDAF6634 CRC64;
MEKHGDYDIK KICVIGLGYI GLPTASMLAN HGYDVVGVDV NEKRVNQIKN GELKIEEPGL
LTLVKGAINS KNLNVRTSAT EADAFIICVP TPALAKEDGS KKCDLSYVMS AVEAILPFVK
DGNLIVIEST IPPETTKKIY ETLNKKIYVA HCPERVLPGK ILKELVENDR IIGGINKKSA
EMAKEIYKSF VEGQIYTTDS NTAEMVKLME NTYRDINIAL ANEFAKICDE IGVNVWDAIK
IANKHPRVNI LNPGPGVGGH CISIDPWFIV EKTNNAKFIR AARELNDNMP AYVCNSVLSE
LKKLGIEKPK ISIFGATYKG NVEDTRESPS KNVIKMLLEN GATVSTYDPH ASYFEYPLST
LDECISGSDC IVVLTDHDVF KTIKKDDIDE ICPKLKNKIV FDTKNILEHS LWKKAGFTVK
LLGNGAW
//
