ID A0A136LR05_9BACT Unreviewed; 416 AA.
AC A0A136LR05;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Vi polysaccharide biosynthesis protein vipA/tviB {ECO:0000313|EMBL:KXK24052.1};
GN ORFNames=UZ12_BCD005002292 {ECO:0000313|EMBL:KXK24052.1};
OS Bacteroidetes bacterium OLB12.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1619897 {ECO:0000313|EMBL:KXK24052.1, ECO:0000313|Proteomes:UP000070129};
RN [1] {ECO:0000313|EMBL:KXK24052.1, ECO:0000313|Proteomes:UP000070129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB12 {ECO:0000313|EMBL:KXK24052.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) 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:KXK24052.1}.
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DR EMBL; LNFR01000080; KXK24052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136LR05; -.
DR STRING; 1619897.UZ12_BCD005002292; -.
DR PATRIC; fig|1619897.3.peg.2506; -.
DR Proteomes; UP000070129; 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: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}.
FT DOMAIN 313..409
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 416 AA; 46136 MW; 9A2F8AE010C993B4 CRC64;
MDKIGVIGLG YVGLPLAVEF GKITDVVGFD INKDRINELK SGVDRTLEVD KAELMSAGKL
TYSFNPEDLK SVKYFIVTVP TPVDEFKTPD LTPLKKASET VGKVLKRGDV VIYESTVYPG
CTEEDCVPVL EKFSGLKFNV DFYCGYSPER INPGDKQHRL PNIKKVTSGS TPEIAEQVDQ
LYKKIIKAGT HKASSIKVAE AAKVIENSQR DINIAFVNEL SLIFEKMGID THEVLEAAGT
KWNFLPYKPG LVGGHCIGVD PYYLTYKADS LGYHPQVILA GRRINDNMGI HIANRVIKLM
TQNDLPVNKA KVLVLGITFK EDCPDIRNSR AIDVIRELQS FGADVEVYDP HADANEVRHE
YGLDLVTQLN KQYAAIVLAV SHAEFRSLNW AAIRGAKTIV YDVKGFLDKS NVTARL
//
