ID V5IN23_NEUCR Unreviewed; 682 AA.
AC V5IN23;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00012954};
DE EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954};
GN ORFNames=NCU04936 {ECO:0000313|EMBL:ESA42780.1};
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110 {ECO:0000313|EMBL:ESA42780.1, ECO:0000313|Proteomes:UP000001805};
RN [1] {ECO:0000313|EMBL:ESA42780.1, ECO:0000313|Proteomes:UP000001805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC {ECO:0000313|Proteomes:UP000001805}, and OR74A
RC {ECO:0000313|EMBL:ESA42780.1};
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA Lander E.S., Nusbaum C., Birren B.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2] {ECO:0000313|EMBL:ESA42780.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR74A {ECO:0000313|EMBL:ESA42780.1};
RG The Broad Institute Genome Sequencing Platform;
RA Galagan J., Henn M.R., Hood H., Radford A., Collins R.A., Walker B.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Allen A.W., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., Chen Z.,
RA Gainer-Dewar J., Gnerre S., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J.B., McCowan C., Murphy C.,
RA Pearson M.D., Poon T.W., Priest M., Roberts A., Saif S., Shea T.D.,
RA Sisk P., Shea T., Sykes S., Zucker J., Kodira C., Bowman B., Colot H.,
RA Ebbole D., Rasmussen C., Baker C., Kalkman E., Chen C.-H., Shi M.,
RA Mathur R., Lambreghts R., Collopy P., Mehra A., Schweredtfeger C., Hong C.,
RA Belden W., Glass N.L., Borkovich K., Dunlap J., Lander E., Wortman J.,
RA Nusbaum C., Sachs M., Birren B.;
RT "The Genome Sequence of Neurospora crassa strain OR74A.";
RL Submitted (APR-2013) 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}.
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DR EMBL; CM002239; ESA42780.1; -; Genomic_DNA.
DR EMBL; CM002239; ESA42781.1; -; Genomic_DNA.
DR RefSeq; XP_011394120.1; XM_011395818.1.
DR RefSeq; XP_011394121.1; XM_011395819.1.
DR AlphaFoldDB; V5IN23; -.
DR STRING; 367110.V5IN23; -.
DR PaxDb; 5141-EFNCRP00000004850; -.
DR EnsemblFungi; ESA42780; ESA42780; NCU04936.
DR EnsemblFungi; ESA42781; ESA42781; NCU04936.
DR GeneID; 3875506; -.
DR KEGG; ncr:NCU04936; -.
DR VEuPathDB; FungiDB:NCU04936; -.
DR HOGENOM; CLU_023810_7_0_1; -.
DR InParanoid; V5IN23; -.
DR OMA; CFIAVGT; -.
DR OrthoDB; 167209at2759; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0006024; P:glycosaminoglycan biosynthetic process; IBA:GO_Central.
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:UP000001805}.
FT DOMAIN 449..555
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 393
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-1"
FT BINDING 209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 249
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 382..386
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 396
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 456
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 463
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
SQ SEQUENCE 682 AA; 73204 MW; A903AE6B2543E88F CRC64;
MAHQLPSTLD LGNDVSLDVS TAPTTPGSNL SFSPVLQAAD EQPGIPAMKP QSTSRSLSST
LFDTTARTPP VRNICCVGAG YVGGPTAAVI AFNNPHIRVT VVDKDEKRIR RWNSVHPPIY
EPGLNHILRI ARDGSKECTI ETRSLSTTNT TSSNTPDVSD ASTPASECGS QCGDNVSKPI
PARQPNLFFT ADVAKSISEA DIVLIAVNTP TKSRGAGAGS ATDMTAFEAV TNVVAQHARP
GAIIVEKSTV PCRTAQFVQD TLALHRPGIH FEVLSNPEFL AAGTAIKDLL NADRILIGSS
ATPSGQRAAA ALASVYSAWI PRSRIITTNV FSSELAKLVA NSMLAQRISS INSIAAVCEV
TGADVSEVAG AIGADPRIGS KFLKAGIGFG GSCFKKDVLS LAYLAESLQL PEVADYWRNV
ITMNEFARNR FASRVVRCLN NTLIGKKLTM LGYAFKKDTN DTRESPAVEI IRTLVEEGPR
EIAVYDPCCN PAQMAEDIGR YVGAEVLQRN GGPVIVYADA YEACHSSDAL LITTEFDEFK
NTGEPVSASA EVLAPKAAPV KAVVPDPRPF KGEEPTETEL LALHTFLLQS TDAEDKEDPL
HRFNSVPDCA EDCPDCFIEK ETGTSGYGAG QEHVFKGRLD WRKVHYHMHK PHWVFDGRGV
LEVAGMEKLG FRVESVGRQG RV
//