IOLJ_BACSU
ID IOLJ_BACSU Reviewed; 290 AA.
AC P42420;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=6-phospho-5-dehydro-2-deoxy-D-gluconate aldolase;
DE Short=DKGP aldolase;
DE EC=4.1.2.29;
GN Name=iolJ; Synonyms=fbaB, yxdI; OrderedLocusNames=BSU39670; ORFNames=B65C;
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 / BGSC1A1;
RX PubMed=7952181; DOI=10.1099/13500872-140-9-2289;
RA Yoshida K., Sano H., Miwa Y., Ogasawara N., Fujita Y.;
RT "Cloning and nucleotide sequencing of a 15 kb region of the Bacillus
RT subtilis genome containing the iol operon.";
RL Microbiology 140:2289-2298(1994).
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 FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=168 / 60015;
RX PubMed=18310071; DOI=10.1074/jbc.m708043200;
RA Yoshida K., Yamaguchi M., Morinaga T., Kinehara M., Ikeuchi M., Ashida H.,
RA Fujita Y.;
RT "Myo-inositol catabolism in Bacillus subtilis.";
RL J. Biol. Chem. 283:10415-10424(2008).
CC -!- FUNCTION: Produces dihydroxyacetone phosphate (DHAP or glycerone
CC phosphate) and malonic semialdehyde (MSA or 3-oxopropanoate) from 6-
CC phospho-5-dehydro-2-deoxy-D-gluconate (DKGP).
CC {ECO:0000269|PubMed:18310071}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-phospho-5-dehydro-2-deoxy-D-gluconate = 3-oxopropanoate +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:13177, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:57642, ChEBI:CHEBI:57949; EC=4.1.2.29;
CC Evidence={ECO:0000269|PubMed:18310071};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC acetyl-CoA from myo-inositol: step 6/7.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. IolJ subfamily. {ECO:0000305}.
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DR EMBL; D14399; BAA03299.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16003.1; -; Genomic_DNA.
DR PIR; B69646; B69646.
DR RefSeq; NP_391846.1; NC_000964.3.
DR RefSeq; WP_003242766.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P42420; -.
DR SMR; P42420; -.
DR STRING; 224308.BSU39670; -.
DR PaxDb; P42420; -.
DR PRIDE; P42420; -.
DR EnsemblBacteria; CAB16003; CAB16003; BSU_39670.
DR GeneID; 937601; -.
DR KEGG; bsu:BSU39670; -.
DR PATRIC; fig|224308.179.peg.4292; -.
DR eggNOG; COG0191; Bacteria.
DR InParanoid; P42420; -.
DR OMA; TVGGMED; -.
DR PhylomeDB; P42420; -.
DR BioCyc; BSUB:BSU39670-MON; -.
DR BioCyc; MetaCyc:BSU39670-MON; -.
DR UniPathway; UPA00076; UER00147.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0047441; F:5-dehydro-2-deoxyphosphogluconate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR CDD; cd00947; TBP_aldolase_IIB; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR011289; Fruc_bis_ald_class-2.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR TIGRFAMs; TIGR00167; cbbA; 1.
DR TIGRFAMs; TIGR01859; fruc_bis_ald; 1.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 1: Evidence at protein level;
KW Lyase; Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..290
FT /note="6-phospho-5-dehydro-2-deoxy-D-gluconate aldolase"
FT /id="PRO_0000178706"
FT ACT_SITE 85
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 209..211
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 230..233
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT MOD_RES 233
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 290 AA; 31372 MW; A0FA0B7A831DE100 CRC64;
MAFVSMKELL EDAKREQYAI GQFNINGLQW TKAILQAAQK EQSPVIAAAS DRLVDYLGGF
KTIAAMVGAL IEDMAITVPV VLHLDHGSSA ERCRQAIDAG FSSVMIDGSH QPIDENIAMT
KEVTDYAAKH GVSVEAEVGT VGGMEDGLVG GVRYADITEC ERIVKETNID ALAAALGSVH
GKYQGEPNLG FKEMEAISRM TDIPLVLHGA SGIPQDQIKK AITLGHAKIN INTECMVAWT
DETRRMFQEN SDLYEPRGYL TPGIEAVEET VRSKMREFGS AGKAAKQQVG
