ID R4KMP6_9FIRM Unreviewed; 435 AA.
AC R4KMP6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Nucleotide sugar dehydrogenase {ECO:0000313|EMBL:AGL03954.1};
GN ORFNames=Desgi_4733 {ECO:0000313|EMBL:AGL03954.1};
OS Desulfoscipio gibsoniae DSM 7213.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC Desulfoscipio.
OX NCBI_TaxID=767817 {ECO:0000313|EMBL:AGL03954.1, ECO:0000313|Proteomes:UP000013520};
RN [1] {ECO:0000313|EMBL:AGL03954.1, ECO:0000313|Proteomes:UP000013520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7213 {ECO:0000313|EMBL:AGL03954.1,
RC ECO:0000313|Proteomes:UP000013520};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Parshina S.,
RA Plugge C., Muyzer G., Kuever J., Ivanova A., Nazina T., Klenk H.-P.,
RA Brambilla E., Spring S., Stams A.F., Woyke T.;
RT "Complete sequence of Desulfotomaculum gibsoniae DSM 7213.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003273; AGL03954.1; -; Genomic_DNA.
DR RefSeq; WP_006522200.1; NC_021184.1.
DR AlphaFoldDB; R4KMP6; -.
DR STRING; 767817.Desgi_4733; -.
DR KEGG; dgi:Desgi_4733; -.
DR eggNOG; COG0677; Bacteria.
DR HOGENOM; CLU_023810_3_2_9; -.
DR OrthoDB; 9803238at2; -.
DR Proteomes; UP000013520; Chromosome.
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:UP000013520};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 329..425
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 435 AA; 48266 MW; 814A0B24F63323BB CRC64;
MSKLKQKIQN KTATLGVVGL GYVGLPLAVE KAKAGYKTIG FDVQESKVKM VNCGKNYIGD
VVNEDLEAIV KSGFLSATTD FAKVAQADCV CICVPTPLDA HQQPVISYVK ASAQSILLYM
HKDMLIVLES TTYPGTTKEL LKPIFESSGL KCGKDFYLAF SPERVDPGNL FYKVKNTPKV
VGGITPECTD IAATLYESVL EAPIHRVSSP TIAEMEKILE NAYRNINIGL INELAILCNR
MGISIWEVID AAKTKPYGFQ AFYPGAGVGG HCIPLDPYYL SWKAREYGFH TSMIEASMII
NDRMPEYCVE RASKILNRDK KAHNGSKILV LGVAYKQDID DYRESPALKV IDILKETGAS
VDYYDPYISE YRYKGEIFKG LESIDADMLK SYDLIVITAS HSNVDYDFVA ANSKWVFDTK
NATKNVQNRN NIILL
//
