UDG_STREE
ID UDG_STREE Reviewed; 394 AA.
AC Q57346; P72519; Q54610;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=UDP-glucose 6-dehydrogenase;
DE Short=UDP-Glc dehydrogenase;
DE Short=UDP-GlcDH;
DE Short=UDPGDH;
DE EC=1.1.1.22;
GN Name=cap3A; Synonyms=cps3D;
OS Streptococcus pneumoniae.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=406 / Type 3;
RX PubMed=7929009; DOI=10.1128/jb.176.20.6375-6383.1994;
RA Arrecubieta C., Lopez R., Garcia E.;
RT "Molecular characterization of cap3A, a gene from the operon required for
RT the synthesis of the capsule of Streptococcus pneumoniae type 3: sequencing
RT of mutations responsible for the unencapsulated phenotype and localization
RT of the capsular cluster on the pneumococcal chromosome.";
RL J. Bacteriol. 176:6375-6383(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=406 / Type 3;
RX PubMed=8566758; DOI=10.1016/0378-1119(95)00657-5;
RA Arrecubieta C., Garcia E., Lopez R.;
RT "Sequence and transcriptional analysis of a DNA region involved in the
RT production of capsular polysaccharide in Streptococcus pneumoniae type 3.";
RL Gene 167:1-7(1995).
RN [3]
RP SEQUENCE REVISION TO 129 AND 228.
RA Garcia E., Arrecubieta C., Munoz R., Mollerach M., Lopez R.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WU2 / Serotype 3;
RX PubMed=7869055; DOI=10.1084/jem.181.3.973;
RA Dillard J.P., Vandersea M.W., Yother J.;
RT "Characterization of the cassette containing genes for type 3 capsular
RT polysaccharide biosynthesis in Streptococcus pneumoniae.";
RL J. Exp. Med. 181:973-983(1995).
CC -!- FUNCTION: Catalyzes the formation of UDP-glucuronic acid which is
CC required for capsular hyaluronic acid synthesis. Directly responsible
CC for the transformation of some unencapsulated serotype-3 SP mutants to
CC the encapsulated phenotype.
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 -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate
CC biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step
CC 1/1.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; Z47210; CAA87403.1; -; Genomic_DNA.
DR EMBL; Z12159; CAA78147.1; -; Genomic_DNA.
DR EMBL; U15171; AAC43311.1; -; Genomic_DNA.
DR AlphaFoldDB; Q57346; -.
DR SMR; Q57346; -.
DR BioCyc; MetaCyc:MON-18145; -.
DR UniPathway; UPA00038; UER00491.
DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
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 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; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52413; SSF52413; 1.
DR TIGRFAMs; TIGR03026; NDP-sugDHase; 1.
PE 3: Inferred from homology;
KW Capsule biogenesis/degradation; NAD; Oxidoreductase.
FT CHAIN 1..394
FT /note="UDP-glucose 6-dehydrogenase"
FT /id="PRO_0000074053"
FT ACT_SITE 259
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 2..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 29
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 83
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 118
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 141..145
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 145
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 248..252
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 258
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 262
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 320
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT CONFLICT 215
FT /note="R -> A (in Ref. 4; AAC43311)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="Y -> D (in Ref. 4; AAC43311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 44697 MW; C68671ED88140FC3 CRC64;
MKIAIAGSGY VGLSLAVLLA QHHEVKVIDV IKDKVESINN RKSPIKDEAI EKYLVEKELN
LEASLDPAHV YKDVEYAIIA TPTNYDVDLN QFDTSSVEAA IKTCMEYNDT CTIVIKSTIP
EGYTKEVREK FNTDRIIFSP EFLRESKALY DNLYPSRIVV GTDLDDSELT KRAWQFADLL
KGGAIKEEVP ILVVAFNEAE VAKLFSNTYL ATRVRYFNEI DTYSEVKGLN PKTIIDIVCY
DPRIGSYYNN PSFGYGGYCL PKDTKQLKAS FRDVPENLIT AVVQSNKTRK DYIAGAILAK
QPSVVGIYRL IMKSDSDNFR SSAVKGVMER LDNYGKEIVI YEPTIECDTF MGYRVIKSLD
EFKNISDIVV ANRMNDDLRD IQEKLYTRDL FGRE
