ALF1_STACT
ID ALF1_STACT Reviewed; 296 AA.
AC Q07159; B9DJW7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Fructose-bisphosphate aldolase class 1;
DE EC=4.1.2.13;
DE AltName: Full=Fructose-bisphosphate aldolase class I;
DE Short=FBP aldolase;
GN Name=fda; OrderedLocusNames=Sca_2144;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-8.
RX PubMed=8226699; DOI=10.1128/jb.175.22.7495-7499.1993;
RA Witke C., Goetz F.;
RT "Cloning, sequencing, and characterization of the gene encoding the class I
RT fructose-1,6-bisphosphate aldolase of Staphylococcus carnosus.";
RL J. Bacteriol. 175:7495-7499(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
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 -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; X71729; CAA50663.1; -; Genomic_DNA.
DR EMBL; AM295250; CAL29049.1; -; Genomic_DNA.
DR PIR; A49943; A49943.
DR RefSeq; WP_015901385.1; NC_012121.1.
DR AlphaFoldDB; Q07159; -.
DR SMR; Q07159; -.
DR STRING; 396513.SCA_2144; -.
DR PRIDE; Q07159; -.
DR GeneID; 60544147; -.
DR KEGG; sca:SCA_2144; -.
DR eggNOG; COG3588; Bacteria.
DR HOGENOM; CLU_081560_0_0_9; -.
DR OMA; GVFGTKM; -.
DR OrthoDB; 945470at2; -.
DR BioCyc; SCAR396513:SCA_RS10820-MON; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000000444; 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 1: Evidence at protein level;
KW Direct protein sequencing; Glycolysis; Lyase; Schiff base.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8226699"
FT CHAIN 2..296
FT /note="Fructose-bisphosphate aldolase class 1"
FT /id="PRO_0000216909"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 212
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000250"
SQ SEQUENCE 296 AA; 32851 MW; 13B5033BE67BF7E9 CRC64;
MNQEQFDKIK NGKGFIAALD QSGGSTPKAL KDYGVEENEY SNDEEMFNLV HDMRTRIITS
PAFNGEKILG AILFEQTMDR EVEGKYTGSY LADKGIVPFL KVDKGLAEEA DGVQLMKPIP
DLDKLLDRAN ERGIFGTKMR SNILENNKEA IEKVVKQQFE VAKEIIAAGL VPIIEPEVNI
NAKDKEAIEA NLAEAIKAEL DNLKKDQYVM LKLTIPTKVN AYSELIEHPQ VIRVVALSGG
YSRDEANKIL KQNDGLIASF SRALVSDLNA QQSDAEFNEK LQEAIDTIFD ASVNKA
