ALF1_STAA3
ID ALF1_STAA3 Reviewed; 296 AA.
AC Q2FDQ4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Fructose-bisphosphate aldolase class 1 {ECO:0000255|HAMAP-Rule:MF_00729};
DE EC=4.1.2.13 {ECO:0000255|HAMAP-Rule:MF_00729};
DE AltName: Full=Fructose-bisphosphate aldolase class I;
DE Short=FBP aldolase {ECO:0000255|HAMAP-Rule:MF_00729};
GN Name=fda {ECO:0000255|HAMAP-Rule:MF_00729};
GN OrderedLocusNames=SAUSA300_2540;
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00729};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC {ECO:0000255|HAMAP-Rule:MF_00729}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000255|HAMAP-Rule:MF_00729}.
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DR EMBL; CP000255; ABD21309.1; -; Genomic_DNA.
DR RefSeq; WP_001031413.1; NZ_CP027476.1.
DR AlphaFoldDB; Q2FDQ4; -.
DR SMR; Q2FDQ4; -.
DR PRIDE; Q2FDQ4; -.
DR EnsemblBacteria; ABD21309; ABD21309; SAUSA300_2540.
DR KEGG; saa:SAUSA300_2540; -.
DR HOGENOM; CLU_081560_0_0_9; -.
DR OMA; GVFGTKM; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000001939; Chromosome.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00729; FBP_aldolase_1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR InterPro; IPR023014; FBA_I_Gram+-type.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
PE 3: Inferred from homology;
KW Glycolysis; Lyase; Schiff base.
FT CHAIN 1..296
FT /note="Fructose-bisphosphate aldolase class 1"
FT /id="PRO_1000045917"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00729"
FT ACT_SITE 212
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00729"
SQ SEQUENCE 296 AA; 33055 MW; 610A2E2FBDA7EB5F CRC64;
MNKEQLEKMK NGKGFIAALD QSGGSTPKAL KEYGVNEDQY SNEDEMFQLV HDMRTRVVTS
PSFSPDKILG AILFEQTMDR EVESKYTADY LADKGVVPFL KVDKGLAEEQ NGVQLMKPID
NLDNLLDRAN ERHIFGTKMR SNILELNEQG IKDVVEQQFE VAKQIIAKGL VPIIEPEVNI
NAKDKAEIEK VLKAELKKGL DSLNADQLVM LKLTIPTEPN LYKELAEHPN VVRVVVLSGG
YSREKANELL KDNAELIASF SRALASDLRA DQSKEEFDKA LGDAVESIYD ASVNKN