(data stored in SCRATCH zone)

SWISSPROT: A0A0E1NX14_YERPA

ID   A0A0E1NX14_YERPA        Unreviewed;       420 AA.
AC   A0A0E1NX14;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   05-DEC-2018, entry version 26.
DE   RecName: Full=UDP-N-acetyl-D-mannosamine dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02029};
DE            EC=1.1.1.336 {ECO:0000256|HAMAP-Rule:MF_02029};
DE   AltName: Full=UDP-ManNAc 6-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02029};
DE   Flags: Precursor;
GN   Name=wecC {ECO:0000256|HAMAP-Rule:MF_02029};
GN   OrderedLocusNames=YPA_0155 {ECO:0000313|EMBL:ABG12124.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12124.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12124.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12124.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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). {ECO:0000256|HAMAP-
CC       Rule:MF_02029}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + 2 NAD(+) + UDP-N-acetyl-alpha-D-mannosamine = 3
CC         H(+) + 2 NADH + UDP-N-acetyl-alpha-D-mannosaminouronate;
CC         Xref=Rhea:RHEA:25780, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:68623,
CC         ChEBI:CHEBI:70731; EC=1.1.1.336; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02029};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial
CC       common antigen biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02029}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02029}.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. WecC subfamily. {ECO:0000256|HAMAP-Rule:MF_02029}.
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DR   EMBL; CP000308; ABG12124.1; -; Genomic_DNA.
DR   RefSeq; WP_002211985.1; NZ_CP009906.1.
DR   SMR; A0A0E1NX14; -.
DR   EnsemblBacteria; ABG12124; ABG12124; YPA_0155.
DR   EnsemblBacteria; AJJ79803; AJJ79803; CH58_2997.
DR   KEGG; ypa:YPA_0155; -.
DR   PATRIC; fig|360102.15.peg.3149; -.
DR   KO; K02472; -.
DR   OMA; VNQHAVD; -.
DR   UniPathway; UPA00566; -.
DR   Proteomes; UP000001971; 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-UniRule.
DR   GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02029; WecC_RffD; 1.
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   InterPro; IPR032891; WecC.
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;
DR   PRODOM; A0A0E1NX14.
DR   SWISS-2DPAGE; A0A0E1NX14.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_02029};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02029}.
FT   NP_BIND      10     15       NAD. {ECO:0000256|HAMAP-Rule:MF_02029}.
FT   REGION      160    161       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02029}.
FT   REGION      216    219       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02029}.
FT   REGION      250    252       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_02029}.
FT   REGION      330    331       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02029}.
FT   ACT_SITE    212    212       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_02029}.
FT   ACT_SITE    266    266       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_02029}.
FT   BINDING     212    212       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02029}.
FT   BINDING     263    263       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02029}.
SQ   SEQUENCE   420 AA;  45639 MW;  BE78C056BD36B453 CRC64;
     MSFETISVIG LGYIGLPTAA AFASRKKKVI GVDVNAHAVE TINRGAIHIV EPDLDKVVKI
     AVEGGYLQAV TKPQAADAFL IAVPTPFKGD HEPDMIFVES AAKSIAPVLK KGDLVILEST
     SPVGATEQMA QWLAEARPDL SFPQQAGEAA DINIAYCPER VLPGQVMVEL IQNDRVIGGM
     TPKCSARASA LYKIFLEGEC VVTNSRTAEM CKLTENSFRD VNIAFANELS LICDEQGINV
     WELIRLANRH PRVNILQPGP GVGGHCIAVD PWFIVSQNPQ LARLIHTARL VNDGKPLWVV
     DRVKAAVADC LAASDKRASE VKIACFGLAF KPDIDDLRES PAVGVARLIA EWHVGETLVV
     EPNVEQLPKS LMGLVTLKDT ATALQQADVL VMLVDHKQFK AIKPEDIKQQ WIVDTKGVWR
//

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