ID   TUAD_BACSU              Reviewed;         461 AA.
AC   O32271;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=UDP-glucose 6-dehydrogenase TuaD;
DE            Short=UDP-Glc dehydrogenase;
DE            Short=UDP-GlcDH;
DE            Short=UDPGDH;
DE            EC=1.1.1.22;
DE   AltName: Full=Teichuronic acid biosynthesis protein TuaD;
GN   Name=tuaD; Synonyms=yvhD; OrderedLocusNames=BSU35580;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=10048024; DOI=10.1046/j.1365-2958.1999.01218.x;
RA   Soldo B., Lazarevic V., Pagni M., Karamata D.;
RT   "Teichuronic acid operon of Bacillus subtilis 168.";
RL   Mol. Microbiol. 31:795-805(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   CHARACTERIZATION.
RC   STRAIN=168;
RX   PubMed=10376820; DOI=10.1099/13500872-145-5-1049;
RA   Pagni M., Lazarevic V., Soldo B., Karamata D.;
RT   "Assay for UDPglucose 6-dehydrogenase in phosphate-starved cells: gene tuaD
RT   of Bacillus subtilis 168 encodes the UDPglucose 6-dehydrogenase involved in
RT   teichuronic acid synthesis.";
RL   Microbiology 145:1049-1053(1999).
RN   [4]
RP   PHOSPHORYLATION, AND ACTIVITY REGULATION.
RX   PubMed=12970183; DOI=10.1093/emboj/cdg458;
RA   Mijakovic I., Poncet S., Boel G., Maze A., Gillet S., Jamet E.,
RA   Decottignies P., Grangeasse C., Doublet P., Le Marechal P., Deutscher J.;
RT   "Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-
RT   glucose dehydrogenases.";
RL   EMBO J. 22:4709-4718(2003).
CC   -!- FUNCTION: Catalyzes the conversion of UDP-glucose into UDP-glucuronate,
CC       one of the precursors of teichuronic acid.
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   -!- ACTIVITY REGULATION: Activated by phosphorylation; inhibited by
CC       dephosphorylation. {ECO:0000269|PubMed:12970183}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By phosphate starvation, via the PhoP/PhoR two-component
CC       regulatory system.
CC   -!- PTM: Phosphorylated by YwqD and dephosphorylated by YwqE in vitro.
CC       {ECO:0000269|PubMed:12970183}.
CC   -!- MISCELLANEOUS: The nature of the anionic polymer present in the cell
CC       wall of B.subtilis depends on phosphate availability. Under phosphate-
CC       replete growth conditions teichoic acids are present, whereas under
CC       phosphate-depleted conditions, at least part of the wall teichoic acid
CC       is replaced with teichuronic acid, a non-phosphate containing anionic
CC       polymer. The synthesis of teichuronic acid is accompanied by
CC       degradation of teichoic acid and reutilization of liberated phosphate
CC       for other cellular processes such as nucleic acid synthesis.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; AF015609; AAB94865.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15575.1; -; Genomic_DNA.
DR   PIR; F69727; F69727.
DR   RefSeq; NP_391438.1; NC_000964.3.
DR   RefSeq; WP_003242596.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O32271; -.
DR   SMR; O32271; -.
DR   STRING; 224308.BSU35580; -.
DR   PaxDb; 224308-BSU35580; -.
DR   EnsemblBacteria; CAB15575; CAB15575; BSU_35580.
DR   GeneID; 936766; -.
DR   KEGG; bsu:BSU35580; -.
DR   PATRIC; fig|224308.179.peg.3849; -.
DR   eggNOG; COG1004; Bacteria.
DR   InParanoid; O32271; -.
DR   OrthoDB; 9803238at2; -.
DR   PhylomeDB; O32271; -.
DR   BioCyc; BSUB:BSU35580-MONOMER; -.
DR   BioCyc; MetaCyc:BSU35580-MONOMER; -.
DR   UniPathway; UPA00038; UER00491.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR   GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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   Cell wall biogenesis/degradation; Cytoplasm; NAD; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Stress response.
FT   CHAIN           1..461
FT                   /note="UDP-glucose 6-dehydrogenase TuaD"
FT                   /id="PRO_0000074075"
FT   ACT_SITE        261
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         3..20
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   BINDING         12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         31
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         122
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         152..156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         156
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         250..254
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         264
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         328
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
SQ   SEQUENCE   461 AA;  49816 MW;  F3B4D189FEC90095 CRC64;
     MKKIAVIGTG YVGLVSGTCF AEIGNKVVCC DIDESKIRSL KNGVIPIYEP GLADLVEKNV
     LDQRLTFTND IPSAIRASDI IYIAVGTPMS KTGEADLTYV KAAAKTIGEH LNGYKVIVNK
     STVPVGTGKL VQSIVQKASK GRYSFDVVSN PEFLREGSAI HDTMNMERAV IGSTSHKAAA
     IIEELHQPFH APVIKTNLES AEMIKYAANA FLATKISFIN DIANICERVG ADVSKVADGV
     GLDSRIGRKF LKAGIGFGGS CFPKDTTALL QIAKSAGYPF KLIEAVIETN EKQRVHIVDK
     LLTVMGSVKG RTISVLGLAF KPNTNDVRSA PALDIIPMLQ QLGAHVKAYD PIAIPEASAI
     LGEQVEYYTD VYAAMEDTDA CLILTDWPEV KEMELVKVKT LLKQPVIIDG RNLFSLEEMQ
     AAGYIYHSIG RPAVRGTEPS DKYFPGLPLE ELAKDLGSVN L
//