ID H5SA79_9DEIN Unreviewed; 443 AA.
AC H5SA79;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 13-SEP-2023, entry version 25.
DE SubName: Full=UDP-N-acetyl-D-mannosamine 6-dehydrogenase {ECO:0000313|EMBL:BAL53099.1};
GN ORFNames=HGMM_F04D06C38 {ECO:0000313|EMBL:BAL53099.1};
OS uncultured Deinococcota bacterium.
OC Bacteria; Deinococcota; environmental samples.
OX NCBI_TaxID=179882 {ECO:0000313|EMBL:BAL53099.1};
RN [1] {ECO:0000313|EMBL:BAL53099.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT "Genetic and functional properties of uncultivated thermophilic
RT crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT genome fragments.";
RL Environ. Microbiol. 7:1967-1984(2005).
RN [2] {ECO:0000313|EMBL:BAL53099.1}
RP NUCLEOTIDE SEQUENCE.
RA Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S.,
RA Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.;
RT "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA
RT Pathway Dominates a Subsurface Ecosystem.";
RL PLoS ONE 7:e30559-e30559(2012).
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; AP011647; BAL53099.1; -; Genomic_DNA.
DR AlphaFoldDB; H5SA79; -.
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}.
FT DOMAIN 335..430
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 443 AA; 48935 MW; FEB43C29C2191238 CRC64;
MTASETHLQA LKGKITNRTA IVGVVGLGYV GLPFAVEKAK VGFRVLGVEQ NPRRAELVNR
GESYIADVPT EVLKEVVDKG LLRAETGFDR MAEMDVIVIA VPTPLTRNLT PDLQYVERVT
REIAPRLRPG QLISLESTTY PGTTEEVMLP ILEGSGLKVE EDFFLVHSPE RVDPGNKRYT
TKNTTKVVGG VGPRSLEAGV FFYSQTIEKV VPVSSAKAAE LVKVFENTFR AVNIALVNEL
AMLCDRMGLN VWEVLDAAFT KPFGIMSFYP GPGVGGHCIP IDPHYLEWKA KEYNFNTHFI
ALAGEINRKM PEFTVEKALR VLAEAGVPLR GAKVLVLGVA YKKDIPDYRE SPAIEVIRGL
RRLGAEVEYH DPHVPRFAEG GLAMESVPLS EERVREKDLV LIATDHSAFD YKAIVAQARR
VLDARGATRH LPRELTEGKV VLL
//
