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Database: UniProt
Entry: Q7MVC7_PORGI
LinkDB: Q7MVC7_PORGI
Original site: Q7MVC7_PORGI 
ID   Q7MVC7_PORGI            Unreviewed;       522 AA.
AC   Q7MVC7;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   13-SEP-2023, entry version 121.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00012954, ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954, ECO:0000256|PIRNR:PIRNR000124};
GN   OrderedLocusNames=PG_1143 {ECO:0000313|EMBL:AAQ66250.1};
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619 {ECO:0000313|EMBL:AAQ66250.1, ECO:0000313|Proteomes:UP000000588};
RN   [1] {ECO:0000313|EMBL:AAQ66250.1, ECO:0000313|Proteomes:UP000000588}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83 {ECO:0000313|Proteomes:UP000000588};
RX   PubMed=12949112; DOI=10.1128/JB.185.18.5591-5601.2003;
RA   Nelson K., Fleishmann R., DeBoy R., Paulsen I., Fouts D., Eisen J.,
RA   Daugherty S., Dodson R., Durkin A., Gwinn M., Haft D., Kolonay J.,
RA   Nelson W., White O., Mason T., Tallon L., Gray J., Granger D., Tettelin H.,
RA   Dong H., Galvin J., Duncan M., Dewhirst F., Fraser C.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
RN   [2] {ECO:0007829|PDB:3GG2}
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 80-518 IN COMPLEX WITH
RP   UDP-ALPHA-D-GLUCURONATE.
RA   Bonanno J.B., Freeman J., Bain K.T., Chang S., Sampathkumar P.,
RA   Wasserman S., Sauder J.M., Burley S.K., Almo S.C.;
RT   "Crystal structure of UDP-glucose 6-dehydrogenase from Porphyromonas
RT   gingivalis bound to product UDP-glucuronate.";
RL   Submitted (FEB-2009) to the PDB data bank.
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; AE015924; AAQ66250.1; -; Genomic_DNA.
DR   PDB; 3GG2; X-ray; 1.70 A; A/B/C/D=80-518.
DR   PDBsum; 3GG2; -.
DR   AlphaFoldDB; Q7MVC7; -.
DR   SMR; Q7MVC7; -.
DR   STRING; 242619.PG_1143; -.
DR   EnsemblBacteria; AAQ66250; AAQ66250; PG_1143.
DR   KEGG; pgi:PG_1143; -.
DR   eggNOG; COG1004; Bacteria.
DR   HOGENOM; CLU_023810_1_2_10; -.
DR   OMA; CECLNLP; -.
DR   UniPathway; UPA00038; UER00491.
DR   EvolutionaryTrace; Q7MVC7; -.
DR   Proteomes; UP000000588; Chromosome.
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.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3GG2};
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:UP000000588}.
FT   DOMAIN          398..500
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
FT   ACT_SITE        344
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-1"
FT   BINDING         88
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         108
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         113
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         164
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         199
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         232
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         233..236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         233
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         234
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         236
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         236
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         244
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         245
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         272
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         275
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         288
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         292
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         328
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         333..337
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         333
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         335
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         335
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         341
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         341
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         344
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         347
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         404
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         405
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         405
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         412
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         470
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0007829|PDB:3GG2"
FT   BINDING         495
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3GG2"
SQ   SEQUENCE   522 AA;  57919 MW;  6A5EE9F8838C7D51 CRC64;
     MGQACIGSRP ISFLWEVRKC RRFIGSYTII RRVIVSHVLS GSRHYIPATG RGNSRLSLDK
     ASPFYLTFVP KNSISYYNMD IAVVGIGYVG LVSATCFAEL GANVRCIDTD RNKIEQLNSG
     TIPIYEPGLE KMIARNVKAG RLRFGTEIEQ AVPEADIVFI AVGTPAGEDG SADMGYVLDA
     ARSIGRAMSR YILIVTKSTV PVGSYRLIRK VIQEELDKRE VLIDFDIASN PEFLKEGNAI
     DDFMKPDRVV VGVDSDRARE LITSLYKPML LNNFRVLFMD IASAEMTKYA ANAMLATRIS
     FMNDVANLCE RVGADVSMVR LGIGSDSRIG SKFLYPGCGY GGSCFPKDVK ALIRTAEDNG
     YRMEVLEAVE RVNEKQKSIL FDKFSTYYKG NVQGRCVAIW GLSFKPGTDD MREAPSLVLI
     EKLLEVGCRV RVYDPVAMKE AQKRLGDKVE YTTDMYDAVR GAEALFHVTE WKEFRMPDWS
     ALSQTMAASL VIDGRNVYEL PADSDFTLLN IGNSAIESAS SK
//
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