(data stored in SCRATCH zone)

SWISSPROT: HPS_BACSU

ID   HPS_BACSU               Reviewed;         210 AA.
AC   P42405; O31477;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   11-DEC-2019, entry version 117.
DE   RecName: Full=3-hexulose-6-phosphate synthase;
DE            Short=HPS;
DE            EC=4.1.2.43;
DE   AltName: Full=D-arabino-3-hexulose-6-phosphate formaldehyde lyase;
DE   AltName: Full=HUMPS;
GN   Name=hxlA; Synonyms=yckG; OrderedLocusNames=BSU03460;
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=7704255; DOI=10.1099/13500872-141-2-277;
RA   Fujishima Y., Yamane K.;
RT   "A 10 kb nucleotide sequence at the 5' flanking region (32 degrees) of
RT   srfAA of the Bacillus subtilis chromosome.";
RL   Microbiology 141:277-279(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA   Yamane K., Kumano M., Kurita K.;
RT   "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT   determination of the sequence of a 146 kb segment and identification of 113
RT   genes.";
RL   Microbiology 142:3047-3056(1996).
RN   [3]
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   [4]
RP   CHARACTERIZATION.
RC   STRAIN=168;
RX   PubMed=10572115;
RA   Yasueda H., Kawahara Y., Sugimoto S.;
RT   "Bacillus subtilis yckG and yckF encode two key enzymes of the ribulose
RT   monophosphate pathway used by methylotrophs, and yckH is required for their
RT   expression.";
RL   J. Bacteriol. 181:7154-7160(1999).
CC   -!- FUNCTION: Catalyzes the condensation of ribulose 5-phosphate with
CC       formaldehyde to form 3-hexulose 6-phosphate. Together with HxlB, may
CC       act as a formaldehyde detoxification system.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 5-phosphate + formaldehyde = D-arabino-hex-3-ulose
CC         6-phosphate; Xref=Rhea:RHEA:25201, ChEBI:CHEBI:16842,
CC         ChEBI:CHEBI:58121, ChEBI:CHEBI:58542; EC=4.1.2.43;
CC   -!- PATHWAY: One-carbon metabolism; formaldehyde assimilation via RuMP
CC       pathway; D-fructose 6-phosphate from D-ribulose 5-phosphate and
CC       formaldehyde: step 1/2.
CC   -!- INDUCTION: By formaldehyde, under the control of HxlR. Not induced by
CC       methanol, formate, or methylamine.
CC   -!- SIMILARITY: Belongs to the HPS/KGPDC family. HPS subfamily.
CC       {ECO:0000305}.
DR   EMBL; D30762; BAA06434.1; -; Genomic_DNA.
DR   EMBL; D50453; BAA08980.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12140.1; -; Genomic_DNA.
DR   PIR; A69761; A69761.
DR   RefSeq; NP_388228.1; NC_000964.3.
DR   RefSeq; WP_003246452.1; NZ_JNCM01000030.1.
DR   SMR; P42405; -.
DR   STRING; 224308.BSU03460; -.
DR   PaxDb; P42405; -.
DR   PRIDE; P42405; -.
DR   EnsemblBacteria; CAB12140; CAB12140; BSU03460.
DR   GeneID; 938314; -.
DR   KEGG; bsu:BSU03460; -.
DR   PATRIC; fig|224308.179.peg.363; -.
DR   eggNOG; ENOG4108VA3; Bacteria.
DR   eggNOG; COG0269; LUCA.
DR   HOGENOM; HOG000226072; -.
DR   InParanoid; P42405; -.
DR   KO; K08093; -.
DR   OMA; WMTVICA; -.
DR   PhylomeDB; P42405; -.
DR   BioCyc; BSUB:BSU03460-MONOMER; -.
DR   UniPathway; UPA00294; UER00434.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043801; F:hexulose-6-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019647; P:formaldehyde assimilation via ribulose monophosphate cycle; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   CDD; cd04726; KGPDC_HPS; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR017553; 3-hexulose-6-phosphate_synth.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR041710; HPS/KGPDC.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR03128; RuMP_HxlA; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P42405.
DR   SWISS-2DPAGE; P42405.
KW   Carbohydrate metabolism; Detoxification; Lyase; One-carbon metabolism;
KW   Reference proteome.
FT   CHAIN           1..210
FT                   /note="3-hexulose-6-phosphate synthase"
FT                   /id="PRO_0000212101"
FT   CONFLICT        114
FT                   /note="K -> T (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        166..210
FT                   /note="GGIKLDTLPEVIQQKPDLVIVGGGITSAADKAETASKMKQLIVQG -> AAS
FT                   NLIHCQK (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   210 AA;  22572 MW;  BA9115BA47CBA846 CRC64;
     MELQLALDLV NIPEAIELVK EVEQYIDVVE IGTPVVINEG LRAVKEIKEA FPQLKVLADL
     KIMDAGGYEI MKASEAGADI ITVLGATDDA TIKGAVEEAK KQKKKILVDM INVKDIESRA
     KEIDALGVDY ICVHTGYDLQ AEGKNSFEEL TTIKNTVKNA KTAIAGGIKL DTLPEVIQQK
     PDLVIVGGGI TSAADKAETA SKMKQLIVQG
//

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