ID A0A0F0IKA3_ASPPU Unreviewed; 557 AA.
AC A0A0F0IKA3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00012954};
DE EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954};
GN ORFNames=P875_00117021 {ECO:0000313|EMBL:KJK67581.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK67581.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK67581.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-
CC alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22;
CC Evidence={ECO:0000256|ARBA:ARBA00000874};
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}.
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:KJK67581.1}.
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DR EMBL; JZEE01000188; KJK67581.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0IKA3; -.
DR STRING; 1403190.A0A0F0IKA3; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000033540; 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:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
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; IPR028357; UDPglc_DH_bac.
DR InterPro; IPR028356; UDPglc_DH_euk.
DR NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR PANTHER; PTHR11374:SF57; DEHYDROGENASE UGD1, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G00920)-RELATED; 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; 2.
DR PIRSF; PIRSF500134; UDPglc_DH_bac; 2.
DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 2.
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:PIRSR500134-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000033540};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..557
FT /note="UDP-glucose 6-dehydrogenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002443684"
FT DOMAIN 424..536
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT REGION 120..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 431
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 438
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
SQ SEQUENCE 557 AA; 61423 MW; 8E335CCD4A879961 CRC64;
MPFLPILLVL AGLTLLFRRR RYKAIEQGES PRVVVKGHTY SDSVEEIELP QLKSEKVENV
RKACMIGAGY VGGLTALVLA SQNPHIQFSV VDSDARLIAA WNSDRPPVFE PGLEDLLFEP
IDPPALPTPS PSPKPEASQD EDCLESSSNS NNHGELVALL PRRRKLANVS FSTNMHEAVA
AADMVFLCVD APSSIMNGDK SDIDLFRLEI AIQAIAQVST GHKIIVQKST APCGIVPRLK
KLLKETASPS ASFDVLSNPD FLVPGAAIRD LLYPPRVIIG HVFSEDMSPK ALTALKRLYS
PWVPDDRIVT MDAWSSELGK IAANALLAQQ ISSLNSLSVL CESTNANINY VSETLGLSQR
SGLGFGGSNL QSDVLCLVYL ARELGLQEVV DYWMAVLRMN EYQRHRVVKR LITRLGDVKE
KRVAVLGFVS KGNVMDTRTT TALGLVRTLT SNGVRVNIYD PHVQADRSES TLRLYDCHPE
MVTVTESIET ACFGCSALVL HTDWEEFRQD QVRWQRIAGH MASPRVLLDP HGVFDGFKMQ
QWGFEVLQVG IRSAKVL
//
