ID ALF1_FUSNN Reviewed; 295 AA.
AC Q8RGH3;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 106.
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=FN0322;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
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; AE009951; AAL94528.1; -; Genomic_DNA.
DR RefSeq; NP_603229.1; NC_003454.1.
DR RefSeq; WP_005901613.1; NZ_CP028101.1.
DR AlphaFoldDB; Q8RGH3; -.
DR SMR; Q8RGH3; -.
DR STRING; 190304.FN0322; -.
DR PaxDb; 190304-FN0322; -.
DR EnsemblBacteria; AAL94528; AAL94528; FN0322.
DR GeneID; 79783331; -.
DR KEGG; fnu:FN0322; -.
DR PATRIC; fig|190304.8.peg.902; -.
DR eggNOG; COG3588; Bacteria.
DR HOGENOM; CLU_081560_0_0_0; -.
DR InParanoid; Q8RGH3; -.
DR BioCyc; FNUC190304:G1FZS-919-MONOMER; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000002521; 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; Aldolase class I; 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; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR11627:SF80; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Glycolysis; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..295
FT /note="Fructose-bisphosphate aldolase class 1"
FT /id="PRO_0000216900"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00729"
FT ACT_SITE 213
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00729"
SQ SEQUENCE 295 AA; 32896 MW; 492DA50FBAC26495 CRC64;
MNEKLEKMRN GKGFIAALDQ SGGSTPKALK LYGVNENEYS NDKEMFDLIH KMRTRIIKSP
AFNESKILGA ILFEQTMDSK IDGKYTADFL WEEKKVLPFL KIDKGLNDLD ADGVQTMKPN
PTLADLLKRA NERHIFGTKM RSVIKKASPA GIARVVEQQF EVAAQVVAAG LIPIIEPEVD
INNVDKVQCE EILRDEIRKH LNALPETSNV MLKLTLPTVE NLYEEFTKHP RVVRVVALSG
GYSREKANDI LSKNKGVIAS FSRALTEGLS AQQTDEEFNK TLAASIDGIY EASVK
//
