ID A0A1I4D737_9PROT Unreviewed; 454 AA.
AC A0A1I4D737;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=UDP-N-acetyl-D-glucosamine dehydrogenase {ECO:0000313|EMBL:SFK87791.1};
GN ORFNames=SAMN02745775_109117 {ECO:0000313|EMBL:SFK87791.1};
OS Falsiroseomonas stagni DSM 19981.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Falsiroseomonas.
OX NCBI_TaxID=1123062 {ECO:0000313|EMBL:SFK87791.1, ECO:0000313|Proteomes:UP000199473};
RN [1] {ECO:0000313|EMBL:SFK87791.1, ECO:0000313|Proteomes:UP000199473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19981 {ECO:0000313|EMBL:SFK87791.1,
RC ECO:0000313|Proteomes:UP000199473};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|PIRNR:PIRNR000124}.
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DR EMBL; FOSQ01000009; SFK87791.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4D737; -.
DR STRING; 1123062.SAMN02745775_109117; -.
DR OrthoDB; 9803238at2; -.
DR Proteomes; UP000199473; 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:UP000199473};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 343..443
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 454 AA; 48329 MW; 631CDF7A5D79BC97 CRC64;
MPDTNAAPAT IPLAAAELMR RIEARDAIVG VIGLGYVGLP LALAVAGAGH RVLGFDIDAP
KVAGLNQGRS PLRHIGDAAV AEAVAAGGFA ATADFDRLEE ADLLIICVPT PLDRHREPDL
SFVEGTARAI ARRLRRGQLV VLESTTWPGT TLELVKPILE ATGLLSGHDF FLAYSPERED
PGNPVFTTAA IPKVVGGDGR AALDLASAFY AGVVARVVPV SSAATAEAVK LTENVFRAVN
IALVNELKTI YDAMGIDVWE VIEAASTKPF GFMPFQPGPG LGGHCIPIDP FYLTWKAREY
GINTRFIELA GEVNTLMPRL VVEKLAQALD RQARRGLNGA RILLLGMAYK RNVDDLRESP
SLVLTRLLEA RGAIVDYHDP HVPEVPRTRE HPELAGRRSV PADAGSVAGY DAVLVATDHD
AVDHAAIARA ARLVVDTRNA CARAGVRGPH IVKA
//
