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Database: UniProt
Entry: A0A091NWU6_HALAL
LinkDB: A0A091NWU6_HALAL
Original site: A0A091NWU6_HALAL 
ID   A0A091NWU6_HALAL        Unreviewed;       496 AA.
AC   A0A091NWU6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
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   Name=Ugdh {ECO:0000313|EMBL:NWZ48011.1};
GN   ORFNames=HALALB_R04900 {ECO:0000313|EMBL:NWZ48011.1}, N329_06877
GN   {ECO:0000313|EMBL:KFP97132.1};
OS   Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC   Accipitrinae; Haliaeetus.
OX   NCBI_TaxID=8969 {ECO:0000313|EMBL:KFP97132.1, ECO:0000313|Proteomes:UP000054379};
RN   [1] {ECO:0000313|EMBL:KFP97132.1, ECO:0000313|Proteomes:UP000054379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N329 {ECO:0000313|EMBL:KFP97132.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:NWZ48011.1, ECO:0000313|Proteomes:UP000585422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OUT-0040 {ECO:0000313|EMBL:NWZ48011.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:NWZ48011.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (SEP-2019) 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   -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
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; KK643004; KFP97132.1; -; Genomic_DNA.
DR   EMBL; VZSQ01000020; NWZ48011.1; -; Genomic_DNA.
DR   UniPathway; UPA00038; UER00491.
DR   Proteomes; UP000054379; Unassembled WGS sequence.
DR   Proteomes; UP000585422; 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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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:SF59; 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   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
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:UP000054379}.
FT   DOMAIN          334..449
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
FT   ACT_SITE        278
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         163..167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT   BINDING         167
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         222..226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT   BINDING         269..275
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT   BINDING         278..281
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         340..341
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT   BINDING         348
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         444
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
SQ   SEQUENCE   496 AA;  55195 MW;  F25421425CF3FCEA CRC64;
     MFEIKKICCI GAGYVGGPTC SVIAQMCPSI KVTVVDVNEA RINAWNSETL PIYEPGLKEV
     VESCRGRNLF FSTSIDDAIR EADLVFISVN TPTKTYGMGK GRAADLKYIE ACARRIVQNS
     NGYKIVTEKS TVPVRAAESI RRIFDANTKP NLDLQASVLS NPEFLAEGTA IKDLKNPDRV
     LIGGDDSPEG QKAVRALCAV YEHWVPKEKI LTTNTWSSEL SKLAANAFLA QRISSINSIS
     ALCEATGADV EEVARAIGTD QRIGNKFLKA SVGFGGSCFQ KDVLNLVYLC EALNLPEVAR
     YWQQVIDMND YQRRRFASRI IDSLFNTVTD KKIAILGFAF KKDTGDTRES SSIYISKYLM
     DEGAKLHIYD PKVPKEQIIL DLSHPGVSED NQVSRLVTIS KDPYEACDGA HALVICTEWD
     MFKELDYERI HKKMLKPAFI FDGRRVLDDL HNELQVIGFQ IETIGKKVSA KRIPFASSCE
     IPKFSLQDPP VKKPRV
//
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