ID R9NFR7_9FIRM Unreviewed; 437 AA.
AC R9NFR7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Nucleotide sugar dehydrogenase {ECO:0000313|EMBL:EOS78812.1};
GN ORFNames=C817_03333 {ECO:0000313|EMBL:EOS78812.1};
OS Dorea sp. 5-2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX NCBI_TaxID=1235798 {ECO:0000313|EMBL:EOS78812.1, ECO:0000313|Proteomes:UP000014211};
RN [1] {ECO:0000313|EMBL:EOS78812.1, ECO:0000313|Proteomes:UP000014211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-2 {ECO:0000313|EMBL:EOS78812.1,
RC ECO:0000313|Proteomes:UP000014211};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., 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 Dorea bacterium 5-2.";
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:EOS78812.1}.
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DR EMBL; ASTD01000063; EOS78812.1; -; Genomic_DNA.
DR RefSeq; WP_016220030.1; NZ_KE159794.1.
DR AlphaFoldDB; R9NFR7; -.
DR STRING; 1235798.C817_03333; -.
DR PATRIC; fig|1235798.3.peg.3506; -.
DR eggNOG; COG0677; Bacteria.
DR HOGENOM; CLU_023810_3_2_9; -.
DR OrthoDB; 9803238at2; -.
DR Proteomes; UP000014211; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000014211};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 331..427
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 437 AA; 49058 MW; 97AEF33EE09702BE CRC64;
MKEYMLKKIS DKSIVVGVVG LGYVGLPLAV EKAKAGYKTI GFDVQFQKVD MVNKGQNYIG
DVVDRELVNL VDSGNLEATT DFSFVKNVDF IAICVPTPLD KHQQPDISYV KNSAEEIAKY
LTKKTIVVLE STTYPGTTED LVKPILEEGS GLKCGVDFYL GFSPERVDPG NIIYKTKNTP
KVVGGVGKDA TEVIAAMYRS VLEGEVKEVS SPTIAEMEKI LENTYRNVNI GMINELAMLC
DRMGINIWEV IEAAKTKPYG FQAFYPGPGL GGHCIPLDPY YLSWKAREYG FHTSMIESSM
SINDKMPEYC VGRAVRILNK YEKSLKMAKI LVVGVAYKQN IDDYRESPAL EVIKILEESG
ALVEFYDPWI SEYKYQGKIH KGKQNIKPEQ VEKYDLLIIT AAHSNVDYVM LQKHAKNIFD
TKNVMKDIKN RENIEVL
//
