ID A0A151WUA5_9HYME Unreviewed; 480 AA.
AC A0A151WUA5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 13-SEP-2023, entry version 22.
DE RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00015132, ECO:0000256|PIRNR:PIRNR000124};
DE EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954, ECO:0000256|PIRNR:PIRNR000124};
GN ORFNames=ALC60_09680 {ECO:0000313|EMBL:KYQ51215.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ51215.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ51215.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ51215.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ51215.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of glycosaminoglycans;
CC hyaluronan, chondroitin sulfate, and heparan sulfate.
CC {ECO:0000256|PIRNR:PIRNR000124}.
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 ECO:0000256|PIRNR:PIRNR000124};
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ982753; KYQ51215.1; -; Genomic_DNA.
DR RefSeq; XP_018309379.1; XM_018453877.1.
DR AlphaFoldDB; A0A151WUA5; -.
DR STRING; 64791.A0A151WUA5; -.
DR GeneID; 108726371; -.
DR OrthoDB; 167209at2759; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000075809; 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|PIRNR:PIRNR000124};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000124};
KW Reference proteome {ECO:0000313|Proteomes:UP000075809}.
FT DOMAIN 332..448
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT ACT_SITE 276
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-1"
FT BINDING 11..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 41
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 89..93
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 130..131
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 165
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 276..279
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 346
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
SQ SEQUENCE 480 AA; 53059 MW; 5BD372D5182DEC8F CRC64;
MTRIRRICCI GAGYVGGPTC SVIALKCPEI QVTVVDKSKE RIAQWNSQKL PIYEPGLDEV
VGKCRGKNLF FSTDIDTAIK EADLIFISVN TPTKTFGNGK GRAADLKYVE SAARMIAQVA
TGDKIVVEKS TVPVRAAESI MNILRANHKP GVSYQILSNP EFLAEGTAIE DLVNADRVLI
GGENSPEGQA AIEELCQIYE HWIPREKILT TNTWSSELSK LAANAFLAQR ISSINSLSAV
CEATGADVSE VARAIGLDSR IGSKFLSASV GFGGSCFQKD ILNLVYICEC LNLPEVAAYW
QQVIDMNEYQ KSRFSAKVIE SLFNTVTDKR IAMLGFAFKK DTGDTRESPA IHVAKTLLDE
GAVLHIYDPK VEETQIIQDL THPSITSNPK DVKSRISIYK DAYSATKNTH AIVLCTEWDE
FIELDYTQIY ADMMKPAYIF DGRNILNFDR LQRIGFIVQT IGKKRTRSGI SRAWGSQTQI
//
