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Database: UniProt
Entry: D3P5C9_AZOS1
LinkDB: D3P5C9_AZOS1
Original site: D3P5C9_AZOS1 
ID   D3P5C9_AZOS1            Unreviewed;       443 AA.
AC   D3P5C9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 71.
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=ugd {ECO:0000313|EMBL:BAI75858.1};
GN   OrderedLocusNames=AZL_d00320 {ECO:0000313|EMBL:BAI75858.1};
OS   Azospirillum sp. (strain B510).
OG   Plasmid pAB510d {ECO:0000313|EMBL:BAI75858.1,
OG   ECO:0000313|Proteomes:UP000002040}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI75858.1, ECO:0000313|Proteomes:UP000002040};
RN   [1] {ECO:0000313|EMBL:BAI75858.1, ECO:0000313|Proteomes:UP000002040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B510 {ECO:0000313|EMBL:BAI75858.1,
RC   ECO:0000313|Proteomes:UP000002040};
RC   PLASMID=pAB510d {ECO:0000313|EMBL:BAI75858.1};
RX   PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA   Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA   Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA   Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA   Nakayama S., Yamada M., Tabata S., Sato S.;
RT   "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT   sp. B510.";
RL   DNA Res. 17:37-50(2010).
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}.
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DR   EMBL; AP010950; BAI75858.1; -; Genomic_DNA.
DR   RefSeq; WP_012977667.1; NC_013858.1.
DR   AlphaFoldDB; D3P5C9; -.
DR   KEGG; azl:AZL_d00320; -.
DR   HOGENOM; CLU_023810_1_2_5; -.
DR   OrthoDB; 9803238at2; -.
DR   UniPathway; UPA00038; UER00491.
DR   Proteomes; UP000002040; Plasmid pAB510d.
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   NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR   PANTHER; PTHR43750; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 1.
DR   PANTHER; PTHR43750:SF3; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 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; PIRSF500134; UDPglc_DH_bac; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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}; Plasmid {ECO:0000313|EMBL:BAI75858.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002040}.
FT   DOMAIN          317..418
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
FT   ACT_SITE        263
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-1"
FT   BINDING         30
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         86
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         122
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         152..155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         155
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         252..256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         266
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         331
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
SQ   SEQUENCE   443 AA;  47872 MW;  ED41A9AB5CB10753 CRC64;
     MRIAMIGTGY VGLVSGACFS EFGVHVTCVD KDAGKIERLK NGEIPIYEPG LDDLVARNVA
     AGRLSFTLDL KEAMQGVDAV FIAVGTPSRR GDGHADLSYV YGAAEEIARN LDHYTVVVTK
     STVPVGTGRE VEAIIRRVRP DAEFDVASNP EFLREGSAIG DFMRPDRVVI GATSDRAGEV
     MRRLYRPLYL IETPIVVTSL ETAELTKYAA NTFLAAKITF INEIADLCEK VGANVHDVAR
     GIGLDGRIGK KFLHPGPGYG GSCFPKDTLA LVRTAQQVGS PLRIIETVVD INDKRKKQMA
     ERIIAACGGS VDGKTVAVLG VAFKPNTDDM RDSPSLDIVP ALQAAGAHVR AFDPAAMREA
     EKLLPGVEWA RDAYGTLEGA DCVAILTEWN EFRALDLRRV KSMLKRPVMI DLRNIYNPDD
     MAKAGFTYSS IGRPTPAGGM DRG
//
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