ID   NTDC_BACSU              Reviewed;         350 AA.
AC   O07564; Q796S2;
DT   02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Glucose-6-phosphate 3-dehydrogenase;
DE            EC=1.1.1.361;
GN   Name=ntdC; Synonyms=yhjJ; OrderedLocusNames=BSU10530;
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=9579061; DOI=10.1099/00221287-144-4-859;
RA   Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA   Venema G., Bron S.;
RT   "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT   subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT   many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL   Microbiology 144:859-875(1998).
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   SEQUENCE REVISION TO 227.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   FUNCTION IN THE NEOTREHALOSADIAMINE BIOSYNTHESIS, AND INDUCTION.
RC   STRAIN=168 / 61884;
RX   PubMed=14612444; DOI=10.1074/jbc.m309925200;
RA   Inaoka T., Takahashi K., Yada H., Yoshida M., Ochi K.;
RT   "RNA polymerase mutation activates the production of a dormant antibiotic
RT   3,3'-neotrehalosadiamine via an autoinduction mechanism in Bacillus
RT   subtilis.";
RL   J. Biol. Chem. 279:3885-3892(2004).
RN   [5]
RP   INDUCTION.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=17056753; DOI=10.1128/jb.01478-06;
RA   Inaoka T., Ochi K.;
RT   "Glucose uptake pathway-specific regulation of synthesis of
RT   neotrehalosadiamine, a novel autoinducer produced in Bacillus subtilis.";
RL   J. Bacteriol. 189:65-75(2007).
RN   [6]
RP   FUNCTION IN THE KANOSAMINE BIOSYNTHESIS AND AS A DEHYDROGENASE, CATALYTIC
RP   ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=23586652; DOI=10.1021/ja4010255;
RA   Vetter N.D., Langill D.M., Anjum S., Boisvert-Martel J., Jagdhane R.C.,
RA   Omene E., Zheng H., van Straaten K.E., Asiamah I., Krol E.S., Sanders D.A.,
RA   Palmer D.R.;
RT   "A previously unrecognized kanosamine biosynthesis pathway in Bacillus
RT   subtilis.";
RL   J. Am. Chem. Soc. 135:5970-5973(2013).
CC   -!- FUNCTION: Involved in the biosynthesis of kanosamine (3-amino-3-deoxy-
CC       D-glucose), which is known to have antibiotic and antifungal
CC       properties, and to be a precursor of the antibiotic neotrehalosadiamine
CC       (3,3'-diamino-3,3'-dideoxy-alpha,beta-trehalose (NTD)). Catalyzes the
CC       oxidation of glucose 6-phosphate to 3-oxo-D-glucose 6-phosphate. It can
CC       only use NAD. {ECO:0000269|PubMed:14612444,
CC       ECO:0000269|PubMed:23586652}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose 6-phosphate + NAD(+) = 3-dehydro-D-glucose 6-
CC         phosphate + H(+) + NADH; Xref=Rhea:RHEA:37547, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:61548,
CC         ChEBI:CHEBI:75052; EC=1.1.1.361;
CC         Evidence={ECO:0000269|PubMed:23586652};
CC   -!- PATHWAY: Antibiotic biosynthesis; kanosamine biosynthesis.
CC   -!- INDUCTION: Induced by neotrehalosadiamine.
CC       {ECO:0000269|PubMed:14612444, ECO:0000269|PubMed:17056753}.
CC   -!- MISCELLANEOUS: The production of neotrehalosadiamine is dormant in the
CC       wild-type strain. A mutation in the beta subunit of RNA polymerase
CC       activates the production of the neotrehalosadiamine (PubMed:14612444).
CC       {ECO:0000305|PubMed:14612444}.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR   EMBL; Y14081; CAA74472.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12893.2; -; Genomic_DNA.
DR   PIR; A69834; A69834.
DR   RefSeq; NP_388934.2; NC_000964.3.
DR   RefSeq; WP_003244701.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O07564; -.
DR   SMR; O07564; -.
DR   STRING; 224308.BSU10530; -.
DR   PaxDb; O07564; -.
DR   PRIDE; O07564; -.
DR   DNASU; 936337; -.
DR   EnsemblBacteria; CAB12893; CAB12893; BSU_10530.
DR   GeneID; 936337; -.
DR   KEGG; bsu:BSU10530; -.
DR   PATRIC; fig|224308.179.peg.1132; -.
DR   eggNOG; COG0673; Bacteria.
DR   InParanoid; O07564; -.
DR   OMA; DWRVEDK; -.
DR   PhylomeDB; O07564; -.
DR   BioCyc; BSUB:BSU10530-MON; -.
DR   BioCyc; MetaCyc:BSU10530-MON; -.
DR   UniPathway; UPA01036; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0103074; F:glucose-6-phosphate 3-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR   InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..350
FT                   /note="Glucose-6-phosphate 3-dehydrogenase"
FT                   /id="PRO_0000091777"
FT   CONFLICT        227
FT                   /note="K -> R (in Ref. 1; CAA74472)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   350 AA;  39273 MW;  9DE62A2E35A5441E CRC64;
     MKKIGIIGAG GIARAHATAL STIKNAELVG VYDINQQNAE SFVKTFGGKS FENVDELIDA
     SEGLIVASPN FCHKEHALQA LGKHKHVLCE KPMAISLEEA SIMKDTAERL SVRASMGFNY
     RYLSYVNILK SLIINNELGN ILSIKVHFKK NSALRRKKFT WRDDANSKKT SGSLGDLGIH
     LIDMVWYLFE SDFITESVRA KMNTNVKTKE DKQVLVDDYA EIYGQLKNKV FVNIITSKCS
     VPEDCGFSIE VVGHKKEFKY HTGNPHVYKL IDGLNVVDCP VPQSLLNDPP NEFYGWADSF
     RSELINWIAS TQNDWVEIPS FSDGFRSQEV LEMFFEKDSN SQPMSVSAVN