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Database: UniProt
Entry: A0A495SI96_9FLAO
LinkDB: A0A495SI96_9FLAO
Original site: A0A495SI96_9FLAO 
ID   A0A495SI96_9FLAO        Unreviewed;       463 AA.
AC   A0A495SI96;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   13-SEP-2023, entry version 14.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00012954};
DE            EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954};
GN   ORFNames=C8C88_1783 {ECO:0000313|EMBL:RKS99970.1};
OS   Flavobacterium sp. 123.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2135627 {ECO:0000313|EMBL:RKS99970.1, ECO:0000313|Proteomes:UP000271452};
RN   [1] {ECO:0000313|EMBL:RKS99970.1, ECO:0000313|Proteomes:UP000271452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=123 {ECO:0000313|EMBL:RKS99970.1,
RC   ECO:0000313|Proteomes:UP000271452};
RA   Chistoserdova L.;
RT   "Synthetic bacterial communities of pure cultures isolated from sediment of
RT   Lake Washington, USA.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate
CC       biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step
CC       1/1. {ECO:0000256|ARBA:ARBA00004701}.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00006601, 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:RKS99970.1}.
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DR   EMBL; RBXD01000001; RKS99970.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495SI96; -.
DR   OrthoDB; 9803238at2; -.
DR   UniPathway; UPA00038; UER00491.
DR   Proteomes; UP000271452; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
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; IPR028356; UDPglc_DH_euk.
DR   NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR   PANTHER; PTHR11374:SF3; UDP-GLUCOSE 6-DEHYDROGENASE; 1.
DR   PANTHER; PTHR11374; UDP-GLUCOSE DEHYDROGENASE/UDP-MANNAC 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; PIRSF500133; UDPglc_DH_euk; 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, ECO:0000256|PIRSR:PIRSR500133-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271452}.
FT   DOMAIN          333..448
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
FT   ACT_SITE        277
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-1"
FT   BINDING         10..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         40
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         91..95
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         132..133
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         162..166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT   BINDING         166
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         221..225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT   BINDING         268..274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT   BINDING         277..280
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         339..340
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT   BINDING         347
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         443
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
SQ   SEQUENCE   463 AA;  51016 MW;  C4E1F2840824E322 CRC64;
     MKITKICCIG AGYVGGPTMA VIAQKCPQIK VTVVDLNEER ILAWNDPNVD NIPIYEPGLS
     AIVGEARGRN LFFSTEVDKA IDEAQIIFIS VNTPTKTYGK GKGMAADLKY IELCARQIAK
     VAKQNKIVVE KSTLPVRTAE AIKSILDNTG NGVQFQILSN PEFLAEGTAV SDLLNPDRIL
     IGGDTSEEGQ KAIQALVDVY SNWVPNDKIL TTNVWSSELS KLTANAFLAQ RISSINALSE
     LCEKTGADVN EVARAIGMDS RIGPKFLKAS VGFGGSCFQK DILNLVYIAK SYGLNEVADY
     WEQVIIMNDH QKKRFSNRIV QTLYNTVADK KITFLGWAFK KDTNDTRESA AIYVADDLIN
     EHANIAVYDP KVSEKKILAD LDYLETRASE KNAKSISSFD NPYSACADAH AIAVLTEWDE
     FVGYDWKKIY DGMQKPAFIF DGRNLLNKSE LEAIGFVYQA IGS
//
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