ID   YTCA_BACSU              Reviewed;         428 AA.
AC   O34862; Q795N5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=Putative UDP-glucose 6-dehydrogenase YtcA;
DE            Short=UDP-Glc dehydrogenase;
DE            Short=UDP-GlcDH;
DE            Short=UDPGDH;
DE            EC=1.1.1.22;
DE   Flags: Precursor;
GN   Name=ytcA; OrderedLocusNames=BSU30860;
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=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(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).
CC   -!- FUNCTION: Catalyzes the conversion of UDP-glucose into UDP-glucuronate,
CC       one of the precursors of teichuronic acid. {ECO:0000250}.
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; AF008220; AAC00367.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15064.1; -; Genomic_DNA.
DR   PIR; G69988; G69988.
DR   RefSeq; NP_390964.1; NC_000964.3.
DR   RefSeq; WP_004398478.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34862; -.
DR   SMR; O34862; -.
DR   STRING; 224308.BSU30860; -.
DR   PaxDb; 224308-BSU30860; -.
DR   EnsemblBacteria; CAB15064; CAB15064; BSU_30860.
DR   GeneID; 936155; -.
DR   KEGG; bsu:BSU30860; -.
DR   PATRIC; fig|224308.179.peg.3345; -.
DR   eggNOG; COG1004; Bacteria.
DR   InParanoid; O34862; -.
DR   OrthoDB; 9803238at2; -.
DR   PhylomeDB; O34862; -.
DR   BioCyc; BSUB:BSU30860-MONOMER; -.
DR   UniPathway; UPA00038; UER00491.
DR   Proteomes; UP000001570; Chromosome.
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   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; NAD; Oxidoreductase; Reference proteome;
KW   Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..428
FT                   /note="Putative UDP-glucose 6-dehydrogenase YtcA"
FT                   /id="PRO_0000379980"
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         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         118
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         148..152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         152
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         262
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         326
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
SQ   SEQUENCE   428 AA;  46833 MW;  70A68AAE12178384 CRC64;
     MKICVVGAGY VGLTLSAALA SIGHDMICTD KDVKKIGQLK KGVIPFYEPG LSDAILRCGN
     LSFSSEVKSS MEECPVIFIA VGTPPRSDGS ADTKALQSVI GDLSEAIRSY KTIITKSTVP
     PGTNENIAKQ LIASGVSKNL FNIVSNPEFL REGNALYDML HPDKTVIGVQ EEDHVSAAIV
     KSIYKHIDTP FIVTSLAGAE LIKYANNFFL AAKISFINEM ARICEAYQSD ISDISRAIGL
     DPRIGKHFLQ AGIGYGGSCF PKDLQALQFA AQEKNTETFL LRAVQHINDT QLGLYIKKIQ
     SFFETLQGKK AAVLGISFKP NTDDIRNSQA VRLMERLAEL GCDVHAYDPE AVLPEHLRQH
     VTQHSQAFDA IEESDFLFLA TEWSEFLAFD WKKAADIMKG RLVIDGRNVL KKELIEACGL
     ICTGVGRP
//