ID Q9ZIH8_STRP2 Unreviewed; 412 AA.
AC Q9ZIH8; Q04MA7;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 2.
DT 27-MAR-2024, entry version 138.
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=cps2K {ECO:0000313|EMBL:AAD10180.2};
GN OrderedLocusNames=SPD_0326 {ECO:0000313|EMBL:ABJ54329.1};
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153 {ECO:0000313|EMBL:AAD10180.2};
RN [1] {ECO:0000313|EMBL:AAD10180.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D39 {ECO:0000313|EMBL:AAD10180.2};
RX PubMed=10198036;
RA Iannelli F., Pearce B.J., Pozzi G.;
RT "The type 2 capsule locus of Streptococcus pneumoniae.";
RL J. Bacteriol. 181:2652-2654(1999).
RN [2] {ECO:0000313|EMBL:AAD10180.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D39 {ECO:0000313|EMBL:AAD10180.2};
RA Pearce B.J., Iannelli F., Pozzi G.;
RT "Construction of new unencapsulated (rough) recipients for genetic
RT transformation of streptococcus pneumoniae.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ABJ54329.1, ECO:0000313|Proteomes:UP000001452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 {ECO:0000313|EMBL:ABJ54329.1}, and D39 / NCTC 7466
RC {ECO:0000313|Proteomes:UP000001452};
RX PubMed=17041037; DOI=10.1128/JB.01148-06;
RA Lanie J.A., Ng W.L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(2007).
RN [4] {ECO:0000313|EMBL:ABJ54329.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D39 {ECO:0000313|EMBL:ABJ54329.1};
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Rusch D., Podicherti R., Tsui H.-C.T.,
RA Winkler M.E.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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; AF026471; AAD10180.2; -; Genomic_DNA.
DR EMBL; CP000410; ABJ54329.1; -; Genomic_DNA.
DR RefSeq; WP_000685095.1; NZ_CP118288.1.
DR AlphaFoldDB; Q9ZIH8; -.
DR PaxDb; 373153-SPD_0326; -.
DR KEGG; spd:SPD_0326; -.
DR eggNOG; COG1004; Bacteria.
DR HOGENOM; CLU_023810_2_0_9; -.
DR BioCyc; SPNE373153:G1G6V-358-MONOMER; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000001452; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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 NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR PANTHER; PTHR43750:SF2; UDP-GLUCOSE 6-DEHYDROGENASE; 1.
DR PANTHER; PTHR43750; 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; 2.
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 Capsule biogenesis/degradation {ECO:0000256|ARBA:ARBA00022903};
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:UP000001452}.
FT DOMAIN 323..411
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT ACT_SITE 259
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-1"
FT BINDING 29
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 83
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 118
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 142..145
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 145
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 248..252
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 262
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 337
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 412
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
SQ SEQUENCE 412 AA; 46614 MW; 9494EF2ACDDB0B3A CRC64;
MKIAVAGTGY VGLSIAVLLS QQHQVMAVDI IPEKVELINQ RKSPIQDDYI EKYLAKKDLN
LVATLDAKEA YQDADFVVIA APTNYDPKKN FFDTSAVESV IETALKYNPD AIMVIKSTVP
VGYTESARKK FQTENILFSP EFLRESKALY DNLYPSRIIL GTDKNNERLV SAAETFARLL
QEGALKENID TLYMGFTEAE AVKLFANTYL ALRVSYFNEL DTYSEMKGLD TQAIIDGVGL
DPRIGSHYNN PSFGYGGYCL PKDTKQLLAN YEDIPEELIG AIVRSNSTRK DFIADQVLKM
VDYYDYSAHN IFDERVEKDI IIGIYRLTMK SNSDNFRQSS IQGIMKRIKA KGVRVVIYEP
TLESGSTFFG SSVINDLEEF KRLSNAIVAN RYDNSLEDVK EKVYTRDIFE RD
//
