ALF1_STAHJ
ID ALF1_STAHJ Reviewed; 296 AA.
AC Q4L9B6;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 113.
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}; OrderedLocusNames=SH0450;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE03759.1; -; Genomic_DNA.
DR RefSeq; WP_011274776.1; NC_007168.1.
DR AlphaFoldDB; Q4L9B6; -.
DR SMR; Q4L9B6; -.
DR STRING; 279808.SH0450; -.
DR PRIDE; Q4L9B6; -.
DR EnsemblBacteria; BAE03759; BAE03759; SH0450.
DR GeneID; 58063351; -.
DR KEGG; sha:SH0450; -.
DR eggNOG; COG3588; Bacteria.
DR HOGENOM; CLU_081560_0_0_9; -.
DR OMA; GVFGTKM; -.
DR OrthoDB; 945470at2; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000000543; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..296
FT /note="Fructose-bisphosphate aldolase class 1"
FT /id="PRO_0000216912"
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; 32968 MW; 619D6086BE604E71 CRC64;
MNKEQLEKMT NGKGFIAALD QSGGSTPKAL KEYGVNEDEY SNDDEMFQLV HDMRTRVVTS
PSFSPDKILG AILFEQTMDR EVEGKYTGDY LADKGVVPFL KVDKGLAEQQ NGVQLMKPID
DLDDTLDRAV ERHIFGTKMR SNILELNEQG IKDVVEQQFE FAKKIIAKGL VPIIEPEVNI
NAKDKAEIEE VLKAELKKGL DALNDDQLVM LKLTIPTKAN LYKELADHPN VVRVVVLSGG
YSRDEANKLL KDNDELIASF SRALASDLRA SQSQEEFDKA LGDAVDSIYD ASVNKN
