(data stored in ACNUC7421 zone)

SWISSPROT: C5BBB8_EDWI9

ID   C5BBB8_EDWI9            Unreviewed;       420 AA.
AC   C5BBB8;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 56.
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};
GN   Name=wecC {ECO:0000256|HAMAP-Rule:MF_02029};
GN   OrderedLocusNames=NT01EI_0093 {ECO:0000313|EMBL:ACR67353.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67353.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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). {ECO:0000256|HAMAP-
CC       Rule:MF_02029}.
CC   -!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-mannosamine + 2 NAD(+) +
CC       H(2)O = UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH.
CC       {ECO:0000256|HAMAP-Rule:MF_02029}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial
CC       common antigen biosynthesis. {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; CP001600; ACR67353.1; -; Genomic_DNA.
DR   RefSeq; WP_015869572.1; NC_012779.2.
DR   ProteinModelPortal; C5BBB8; -.
DR   STRING; 634503.NT01EI_0093; -.
DR   EnsemblBacteria; ACR67353; ACR67353; NT01EI_0093.
DR   GeneID; 7959812; -.
DR   KEGG; eic:NT01EI_0093; -.
DR   PATRIC; fig|634503.3.peg.87; -.
DR   eggNOG; ENOG4108IJ1; Bacteria.
DR   eggNOG; COG0677; LUCA.
DR   HOGENOM; HOG000153774; -.
DR   KO; K02472; -.
DR   OMA; VNQHAVD; -.
DR   OrthoDB; POG091H047M; -.
DR   UniPathway; UPA00566; -.
DR   Proteomes; UP000001485; 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-HAMAP.
DR   GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_02029; WecC_RffD; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR017476; UDP-Glc/GDP-Man.
DR   InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
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; C5BBB8.
DR   SWISS-2DPAGE; C5BBB8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_02029};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02029,
KW   ECO:0000313|EMBL:ACR67353.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN      324    420       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
FT   NP_BIND      10     15       NAD. {ECO:0000256|HAMAP-Rule:MF_02029}.
FT   ACT_SITE    266    266       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_02029}.
SQ   SEQUENCE   420 AA;  45745 MW;  870B3BCF7790A0C4 CRC64;
     MSFDTISVIG LGYIGLPTAV AFAGCRKQVI GVDVSQHAVE TINRGEIHIV EPDLDRAVKR
     AVEGGFLRAV MRPEPADAFL IAVPTPFKGE HEPDLTYVEA AARSIAPVLK KGDLVILEST
     SPVGATEQMC AWLAECRADL RFPHQDGEQA DIRVAYCPER VLPGKIMVEL LRNDRVIGGM
     TPTCSAQASA LYRLFLEGEC VETNARTAEM CKLTENSFRD VNIAFANELS LICDAQGIDV
     WQLIALANRH PRVNILQPGP GVGGHCIAVD PWFIVAQNPQ LARLIHTARL VNDGKPLWVV
     DRVKAALADC LAAEDKRASE ATIACFGLAF KPDIDDLRES PAMEITEMVA QWHSGTTLVV
     EPNIHQLPVR LAGMAQLTDC TTALAQADVV VLLVDHQPFR ALAPQAVTQR FVVDTKGVWR
//

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