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
//