YWQF_BACSU
ID YWQF_BACSU Reviewed; 440 AA.
AC P96718; Q795B4;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=UDP-glucose 6-dehydrogenase YwqF;
DE Short=UDP-Glc dehydrogenase;
DE Short=UDP-GlcDH;
DE Short=UDPGDH;
DE EC=1.1.1.22;
GN Name=ywqF; OrderedLocusNames=BSU36230;
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=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
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 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).
RN [4]
RP FUNCTION, MUTAGENESIS OF TYR-10, AND PHOSPHORYLATION.
RX PubMed=15741737; DOI=10.1159/000082077;
RA Mijakovic I., Petranovic D., Deutscher J.;
RT "How tyrosine phosphorylation affects the UDP-glucose dehydrogenase
RT activity of Bacillus subtilis YwqF.";
RL J. Mol. Microbiol. Biotechnol. 8:19-25(2004).
CC -!- FUNCTION: Catalyzes the conversion of UDP-glucose into UDP-glucuronate,
CC one of the precursors of teichuronic acid.
CC {ECO:0000269|PubMed:15741737}.
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: Competitively inhibited by UDP-glucose. Activated
CC by phosphorylation, which may increase affinity for NAD(+); inhibited
CC by 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 {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residue(s). Phosphorylated by YwqD and
CC dephosphorylated by YwqE in vitro. {ECO:0000269|PubMed:12970183,
CC ECO:0000269|PubMed:15741737}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; Z92952; CAB07444.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15640.1; -; Genomic_DNA.
DR PIR; A70067; A70067.
DR RefSeq; NP_391504.1; NC_000964.3.
DR RefSeq; WP_003243223.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P96718; -.
DR SMR; P96718; -.
DR STRING; 224308.BSU36230; -.
DR PaxDb; P96718; -.
DR PRIDE; P96718; -.
DR EnsemblBacteria; CAB15640; CAB15640; BSU_36230.
DR GeneID; 936890; -.
DR KEGG; bsu:BSU36230; -.
DR PATRIC; fig|224308.179.peg.3921; -.
DR eggNOG; COG1004; Bacteria.
DR InParanoid; P96718; -.
DR OMA; ICIDTDE; -.
DR PhylomeDB; P96718; -.
DR BioCyc; BSUB:BSU36230-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.
FT CHAIN 1..440
FT /note="UDP-glucose 6-dehydrogenase YwqF"
FT /id="PRO_0000253341"
FT ACT_SITE 260
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 30
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 151..155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 249..253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 327
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT MUTAGEN 10
FT /note="Y->F: 30-fold decrease in activity but no decrease
FT in the overall phosphorylation level."
FT /evidence="ECO:0000269|PubMed:15741737"
SQ SEQUENCE 440 AA; 47784 MW; 1ADA9454EBE1F645 CRC64;
MNITVIGTGY VGLVTGVSLS EIGHHVTCID IDAHKIDEMR KGISPIFEPG LEELMRKNTA
DGRLNFETSY EKGLAQADII FIAVGTPQKS DGHANLEQIT DAAKRIAKHV KRDTVVVTKS
TVPVGTNDLI NGLITEHLAE PVSISVASNP EFLREGSAIY DTFHGDRIVI GTADEKTANT
LEELFRPFQI PIYQTDIRSA EMIKYASNAF LATKISFINE ISNICEKVGA DIEAVAYGMG
QDKRIGSQFL KAGIGYGGSC FPKDTNALVQ IAGNVEHDFE LLKSVIKVNN NQQAMLVDKA
LNRLGGVTGK TIALLGLSFK PNTDDMREAP SIVIADRLAA LDARIRAYDP IAVSHAKHVL
PQAVEYKETI EEAVKGSDAV MILTDWADIK QFPLAAYQDL METPLIFDGR NCYTLDEALA
AGVEYYSVGR KAVVPSGAIQ
