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Database: UniProt
Entry: G8NXK4_GRAMM
LinkDB: G8NXK4_GRAMM
Original site: G8NXK4_GRAMM 
ID   G8NXK4_GRAMM            Unreviewed;       450 AA.
AC   G8NXK4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Nucleotide sugar dehydrogenase {ECO:0000313|EMBL:AEU38999.1};
DE            EC=1.1.1.22 {ECO:0000313|EMBL:AEU38999.1};
GN   OrderedLocusNames=AciX8_4730 {ECO:0000313|EMBL:AEU38999.1};
OS   Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Granulicella.
OX   NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU38999.1, ECO:0000313|Proteomes:UP000007113};
RN   [1] {ECO:0000313|EMBL:AEU38999.1, ECO:0000313|Proteomes:UP000007113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8
RC   {ECO:0000313|Proteomes:UP000007113};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M.,
RA   Haggblom M., Woyke T.;
RT   "Complete sequence of Granulicella mallensis MP5ACTX8.";
RL   Submitted (NOV-2011) 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; CP003130; AEU38999.1; -; Genomic_DNA.
DR   RefSeq; WP_014267870.1; NC_016631.1.
DR   AlphaFoldDB; G8NXK4; -.
DR   STRING; 682795.AciX8_4730; -.
DR   KEGG; gma:AciX8_4730; -.
DR   eggNOG; COG0677; Bacteria.
DR   HOGENOM; CLU_023810_3_2_0; -.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000007113; 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:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:UniProtKB-EC.
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   ECO:0000313|EMBL:AEU38999.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007113};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          345..441
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   450 AA;  49510 MW;  C15F9C54E6DA705F CRC64;
     MIYTSTLPDW LAQVAARETH IAIIGLGYVG LPLALLFAEE RFRVTGLDID AEKVATLNDG
     RSYIHRIEPE HIATAKKAGF RATTDFAALQ ECDAILICVP TPLHPDHTPD MSFVTSTVEA
     LAPHTRAGQL VVLESTTWPG TTDELVVPMI ERLGRNGLRV LRNDDSDDSL EGLMVSFSPE
     REDPGNLITP RREIPKVIGG VDTRATRAAA ALYGAIFNRT VAMSSPAAAE MTKLLENIYR
     CVNIALVNEL KQLCLAMNID IWEVIDAAST KPFGFQAFYP GPGIGGHCIP VDPFYLSWRA
     KQFNQPTRFI ELAGEVNEAM PAFVVHTAER ALGREGKALA GAKVLVLGIA YKRDVDDLRE
     SPALTIFELL ERAGASVSYN DPFFDEVGVG RKYTLKRRST PLDRVGEFDC VLLVTDHSIY
     DYEALVEGSK LFVDTRNATR GMVSEKIVRC
//
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