ID A0A179H0C3_PURLI Unreviewed; 627 AA.
AC A0A179H0C3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00012954};
DE EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954};
GN ORFNames=PLICBS_004776 {ECO:0000313|EMBL:GJN70718.1}, VFPBJ_10152
GN {ECO:0000313|EMBL:OAQ74857.1}, VFPFJ_08773
GN {ECO:0000313|EMBL:OAQ82970.1};
OS Purpureocillium lilacinum (Paecilomyces lilacinus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ82970.1, ECO:0000313|Proteomes:UP000078340};
RN [1] {ECO:0000313|EMBL:OAQ82970.1, ECO:0000313|Proteomes:UP000078340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLBJ-1 {ECO:0000313|EMBL:OAQ74857.1}, and PLFJ-1
RC {ECO:0000313|EMBL:OAQ82970.1};
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT Phytophthora in bio-control Purpureocillium lilacinum.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GJN70718.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 284.36 {ECO:0000313|EMBL:GJN70718.1};
RA Alimu Y., Kusuya Y., Yamamoto T., Shigemune N., Takahashi H., Yaguchi T.;
RT "Tolerabce induction of polyhexamethylene biguanide on Purpureocillium
RT lilacinum strains.";
RL Submitted (DEC-2021) 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:OAQ82970.1}.
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DR EMBL; BQKW01000003; GJN70718.1; -; Genomic_DNA.
DR EMBL; LSBH01000009; OAQ74857.1; -; Genomic_DNA.
DR EMBL; LSBI01000008; OAQ82970.1; -; Genomic_DNA.
DR RefSeq; XP_018175598.1; XM_018325846.1.
DR STRING; 33203.A0A179H0C3; -.
DR GeneID; 28890895; -.
DR KEGG; plj:VFPFJ_08773; -.
DR OMA; CFIAVGT; -.
DR OrthoDB; 167209at2759; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000078240; Unassembled WGS sequence.
DR Proteomes; UP000078340; Unassembled WGS sequence.
DR Proteomes; UP001056679; 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: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; 2.
DR PIRSF; PIRSF500134; UDPglc_DH_bac; 3.
DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 3.
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:UP000078340}.
FT DOMAIN 392..486
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT REGION 99..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 336
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-1"
FT BINDING 66
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 71
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 325..329
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 339
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 406
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
SQ SEQUENCE 627 AA; 67877 MW; E77DDE47220B81F8 CRC64;
MPSLPEAVVD SVSKLGLNGS SEHTNGTFNG DVKVRTICCV GAGYVGGPTA AVIAFQNPHI
KVTVVDRDTT RIRRWNSRHP PIYEPGLHDI VRIARDGSRE TSFSNGPTSD GEGSSSDEGE
TVVPSRPGNL FFTTDVAKSI AEADVVLVAV NTPTKERGVG AGSATDMTAF EAVTGVVAQY
AREGAIIVEK STVPCRTAQL VADTLSMHRP GVHFEILSNP EFLAAGTAVN DLLYPDRILI
GSAPTPSGKK AAEALVGVYA AWVPRERILT TNVWSSELAK LVANSMLAQR ISSINSISAV
CEQTGADVDE VAKAIGVDPR IGNKFLMAGI GFGGSCFKKD VLNLVYLADT MGLPEVGEYW
RQVVKMNEYA RDRFTNRVIK CLNNTLVGKK ITILGYAFKK NTSDTREAPA LEMIKTLLEE
RPREVAVFDP CCNPLVVKNE ILALLGAEVS QRVHVYSNAF DACEGSTAVV IATEFDEFRN
QPAPKPAPAP VPEAAPKMIG RKPNPKSDPR PFTASTPTEN ELLALHKHLV QRATETSPDP
LDRFNVEPSC EADCPDCITE RESEKTGDAT GMGSAEEYKP KERIDWVRIA SSMAKPRWVF
DGRGVIDSRE MVKLGVRVES VGRQHRF
//
