WECC_METMP
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 03-AUG-2022, entry version 118.
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. {ECO:0000269|PubMed:18263721}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000305}.
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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 PRIDE; Q6LZC3; -.
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 OMA; GHCLPID; -.
DR OrthoDB; 41144at2157; -.
DR BioCyc; MMAR267377:MMP_RS03695-MON; -.
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 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 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 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; 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
