ID A7ZNK6_ECO24 Unreviewed; 424 AA.
AC A7ZNK6;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=VI polysaccharide biosynthesis protein VipA/tviB {ECO:0000313|EMBL:ABV17228.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:ABV17228.1};
GN Name=vipA {ECO:0000313|EMBL:ABV17228.1};
GN OrderedLocusNames=EcE24377A_2325 {ECO:0000313|EMBL:ABV17228.1};
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111 {ECO:0000313|EMBL:ABV17228.1, ECO:0000313|Proteomes:UP000001122};
RN [1] {ECO:0000313|Proteomes:UP000001122}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC {ECO:0000313|Proteomes:UP000001122};
RX PubMed=18676672; DOI=10.1128/JB.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|PIRNR:PIRNR000124}.
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; CP000800; ABV17228.1; -; Genomic_DNA.
DR RefSeq; WP_001017959.1; NC_009801.1.
DR AlphaFoldDB; A7ZNK6; -.
DR KEGG; ecw:EcE24377A_2325; -.
DR HOGENOM; CLU_023810_3_1_6; -.
DR Proteomes; UP000001122; 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; IEA:InterPro.
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 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABV17228.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001122}.
FT DOMAIN 317..417
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 424 AA; 47249 MW; F048431E31D5A5B9 CRC64;
MNIDNIKIGI IGLGYVGLPL AVEFGKKYNT VGFDIKQNRI DELKKQMDST LECTADELAS
AKFLHYSCEI EALKACNIFI VTVPTPIDKY KRPDLSPLVS ASKMLSKVIK NGDIIIFEST
VYPGATEEIC VPQIEAGSGL VFNKDFFIGY SPERINPGDK NHRVTNIMKV TSGSTPEAAT
FVDKIYSSII TAGTYKASSI KVAEAAKVIE NTQRDLNIAL INELAIIFNK LGIDTEDVLK
AAGTKWNFLP FRPGLVGGHC IGVDPYYLTH KAQEIGYHPE VILAGRRIND DMARYVASQL
IKEMIKAGIL IDNANILIMG LSFKENCPDI RNTKIIDIIS ELKDYNLNVD VYDPWVSEDE
ALQEYGIEIH STKPSKKYEG IIFAVAHEQF KNMQSIEIKE LQSTKCVTYD LKYILNKSDA
TIRL
//
