TUAD_BACSU
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 03-AUG-2022, entry version 140.
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; Firmicutes; 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; O32271; -.
DR PRIDE; O32271; -.
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 OMA; TMDAWSS; -.
DR PhylomeDB; O32271; -.
DR BioCyc; BSUB:BSU35580-MON; -.
DR BioCyc; MetaCyc:BSU35580-MON; -.
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 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 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 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
