ID R9H6C8_BACT4 Unreviewed; 400 AA.
AC R9H6C8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Nucleotide sugar dehydrogenase {ECO:0000313|EMBL:EOR99468.1};
GN ORFNames=C799_03349 {ECO:0000313|EMBL:EOR99468.1};
OS Bacteroides thetaiotaomicron dnLKV9.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1235785 {ECO:0000313|EMBL:EOR99468.1, ECO:0000313|Proteomes:UP000014207};
RN [1] {ECO:0000313|EMBL:EOR99468.1, ECO:0000313|Proteomes:UP000014207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=dnLKV9 {ECO:0000313|Proteomes:UP000014207};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Kuhn K., Stappenbeck T., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides thetaiotaomicron dnLKV9.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|PIRNR:PIRNR000124}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOR99468.1}.
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DR EMBL; ASSM01000010; EOR99468.1; -; Genomic_DNA.
DR RefSeq; WP_016269026.1; NZ_KE159460.1.
DR AlphaFoldDB; R9H6C8; -.
DR PATRIC; fig|1235785.3.peg.3379; -.
DR HOGENOM; CLU_023810_3_2_10; -.
DR Proteomes; UP000014207; Unassembled WGS sequence.
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:SF1; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..400
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004472501"
FT DOMAIN 311..400
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 400 AA; 44707 MW; FD76545D69AF3A32 CRC64;
MKKVVFLGLG YIGLPTAAVA AAHGFEVIGV DVNPSVVETI NQGKIHIVEP ELGQVVRDVV
QSGKLRAVCK PEAADAFFIV VPTPFKQNHR ADITYVEAAT RSVIPYLQEG NLFVIESTSP
VYTTERMAEV IYKERPELKG KIHIAYCPER VLPGNTLYEL VHNDRVIGGI DPASTEKAIE
FYSAFVQGKL HGTNARTAEM CKLTENSSRD SQIAFANELS MICDKAGINV WELIELANKH
PRVNILQPGC GVGGHCIAVD PWFIVSDYPE QAQLIKRARE TNDYKADWCA NKVLETCQKF
VEQNEREPVV ACMGLAFKPN IDDLRESPAK YIASRIISES RADVLIIEPN ISTHKSFHLT
DYREAYEKAD IIVWLVRHDV FLALPREEGK IELDFCGVRR
//