ID A0A1M4XD45_9FLAO Unreviewed; 463 AA.
AC A0A1M4XD45;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00012954};
DE EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954};
GN ORFNames=SAMN05444377_10212 {ECO:0000313|EMBL:SHE91499.1};
OS Flavobacterium fontis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1124188 {ECO:0000313|EMBL:SHE91499.1, ECO:0000313|Proteomes:UP000184147};
RN [1] {ECO:0000313|EMBL:SHE91499.1, ECO:0000313|Proteomes:UP000184147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25660 {ECO:0000313|EMBL:SHE91499.1,
RC ECO:0000313|Proteomes:UP000184147};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQVQ01000002; SHE91499.1; -; Genomic_DNA.
DR RefSeq; WP_073361235.1; NZ_FQVQ01000002.1.
DR AlphaFoldDB; A0A1M4XD45; -.
DR STRING; 1124188.SAMN05444377_10212; -.
DR OrthoDB; 9803238at2; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000184147; 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:UP000184147}.
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; 50802 MW; 533563AC6C8E1FE8 CRC64;
MKISHICCIG AGYVGGPTMA VIANKCPHIK VTVVDLNAER IARWNDDNVE NIPVYEPGLS
TIVAASRGKN LFFSTEVDKA IDEAQMIFIS VNTPTKTYGT GKGMAADLKY IELCARQIAR
VATTDKIVVE KSTLPVRTAE ALKSILDNTG NGVQYQILSN PEFLAEGTAV EDLLAPDRVL
IGGGTDEAGQ KAIQALVDIY ANWVPKERIL TTNVWSSELS KLTANAFLAQ RVSSINAISE
LCEKTGANVN EVARAIGMDS RIGSKFLKAS VGFGGSCFQK DILNLVYIAK SYGLQEVADY
WEQVIQLNDH QKNRFARNIV STLYNTISGK KIAFLGWAFK KDTNDTRESA AIYVADALMQ
EQAQIAVYDP KVEHPQVLSD LNYLETRDAA SNAALVTSIG DPYAACHEAH AIAIMTEWDE
FKTYDWQKIY DSMLKPAFIF DGRNILDAEA MRVIGFHYQG IGS
//
