ALF_BACSU
ID ALF_BACSU Reviewed; 285 AA.
AC P13243;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Probable fructose-bisphosphate aldolase;
DE Short=FBP aldolase;
DE Short=FBPA;
DE EC=4.1.2.13;
DE AltName: Full=Fructose-1,6-bisphosphate aldolase;
GN Name=fbaA; Synonyms=fba, fba1, tsr; OrderedLocusNames=BSU37120;
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 / JH642;
RX PubMed=2457578; DOI=10.1128/jb.170.9.4194-4208.1988;
RA Trach K., Chapman J.W., Piggot P.J., Lecoq D., Hoch J.A.;
RT "Complete sequence and transcriptional analysis of the spo0F region of the
RT Bacillus subtilis chromosome.";
RL J. Bacteriol. 170:4194-4208(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26, AND SEQUENCE REVISION.
RC STRAIN=168 / JH642;
RX PubMed=1640835; DOI=10.1111/j.1365-2958.1992.tb00855.x;
RA Mitchell C., Morris P.W., Lum L., Spiegelman G., Vary J.C.;
RT "The amino acid sequence of a Bacillus subtilis phosphoprotein that matches
RT an orfY-tsr coding sequence.";
RL Mol. Microbiol. 6:1345-1349(1992).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 1-16, AND PHOSPHORYLATION.
RX PubMed=1556067; DOI=10.1128/jb.174.8.2474-2477.1992;
RA Mitchell C., Morris P.W., Vary J.C.;
RT "Identification of proteins phosphorylated by ATP during sporulation of
RT Bacillus subtilis.";
RL J. Bacteriol. 174:2474-2477(1992).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-212 AND THR-234, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
CC -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone
CC phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate
CC (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and
CC the reverse reaction in glycolysis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC provides a structural contribution. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- PTM: Phosphorylated during sporulation. {ECO:0000269|PubMed:1556067,
CC ECO:0000269|PubMed:17218307}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; M22039; AAA16803.1; -; Unassigned_DNA.
DR EMBL; S42590; AAB22716.1; -; Genomic_DNA.
DR EMBL; Z49782; CAA89873.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15729.1; -; Genomic_DNA.
DR PIR; S55426; D32354.
DR RefSeq; NP_391593.1; NC_000964.3.
DR RefSeq; WP_003243339.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P13243; -.
DR SMR; P13243; -.
DR IntAct; P13243; 1.
DR MINT; P13243; -.
DR STRING; 224308.BSU37120; -.
DR iPTMnet; P13243; -.
DR jPOST; P13243; -.
DR PaxDb; P13243; -.
DR PRIDE; P13243; -.
DR EnsemblBacteria; CAB15729; CAB15729; BSU_37120.
DR GeneID; 937040; -.
DR KEGG; bsu:BSU37120; -.
DR PATRIC; fig|224308.179.peg.4021; -.
DR eggNOG; COG0191; Bacteria.
DR InParanoid; P13243; -.
DR OMA; PRTWGKL; -.
DR PhylomeDB; P13243; -.
DR BioCyc; BSUB:BSU37120-MON; -.
DR SABIO-RK; P13243; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
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:UniProtKB-UniPathway.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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 Direct protein sequencing; Glycolysis; Lyase; Metal-binding;
KW Phosphoprotein; Reference proteome; Sporulation; Zinc.
FT CHAIN 1..285
FT /note="Probable fructose-bisphosphate aldolase"
FT /id="PRO_0000178705"
FT ACT_SITE 85
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 210..212
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 231..234
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT MOD_RES 212
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17218307"
SQ SEQUENCE 285 AA; 30401 MW; 482D3CE048583BCF CRC64;
MPLVSMTEML NTAKEKGYAV GQFNLNNLEF TQAILQAAEE EKSPVILGVS EGAGRYMGGF
KTVVAMVKAL MEEYKVTVPV AIHLDHGSSF ESCAKAIHAG FTSVMIDASH HPFEENVATT
AKVVELAHFH GVSVEAELGT VGGQEDDVIA EGVIYADPKE CQELVERTGI DCLAPALGSV
HGPYKGEPNL GFKEMEEIGK STGLPLVLHG GTGIPTADIK KSISLGTAKI NVNTENQISS
AKAVRETLAA KPDEYDPRKY LGPAREAIKE TVIGKMREFG SSNQA
