ID A0A226I470_9FLAO Unreviewed; 295 AA.
AC A0A226I470;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Fructose-bisphosphate aldolase class 1 {ECO:0000256|HAMAP-Rule:MF_00729};
DE EC=4.1.2.13 {ECO:0000256|HAMAP-Rule:MF_00729};
DE AltName: Full=Fructose-bisphosphate aldolase class I {ECO:0000256|HAMAP-Rule:MF_00729};
DE Short=FBP aldolase {ECO:0000256|HAMAP-Rule:MF_00729};
GN Name=fda {ECO:0000256|HAMAP-Rule:MF_00729};
GN ORFNames=B0A75_06400 {ECO:0000313|EMBL:OXB01524.1};
OS Flavobacterium oncorhynchi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=728056 {ECO:0000313|EMBL:OXB01524.1, ECO:0000313|Proteomes:UP000198336};
RN [1] {ECO:0000313|EMBL:OXB01524.1, ECO:0000313|Proteomes:UP000198336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 59446 {ECO:0000313|EMBL:OXB01524.1,
RC ECO:0000313|Proteomes:UP000198336};
RA Stine C., Li C., Tadesse D.;
RT "Whole genomes of Flavobacteriaceae.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000441, ECO:0000256|HAMAP-
CC Rule:MF_00729};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC {ECO:0000256|ARBA:ARBA00004714, ECO:0000256|HAMAP-Rule:MF_00729}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000256|ARBA:ARBA00010387, ECO:0000256|HAMAP-
CC Rule:MF_00729}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXB01524.1}.
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DR EMBL; MUHA01000007; OXB01524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226I470; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000198336; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_00729};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00729};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00729}.
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00729"
FT ACT_SITE 213
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00729"
SQ SEQUENCE 295 AA; 33065 MW; B56D7546A560FC6B CRC64;
MNNEQLNRMH SGKGFIAALD QSGGSTPKAL AQYGIQENSF SNDEEMYTLV HEMRTRIIKS
PAFDSKYILG AILFENTMDR KIDGLWTADY LWEKKQIVPF LKVDKGLADL ANGVQLMKPI
SNLDELLTRA VERNVFGTKM RSVIKEANAE GIREVVEQQF AVGLQIFKKG LIPIIEPEVD
IYSADKTKSE EILKEEILKQ LKSLDKDVKV MLKLSIPTVN DFYKELMSSP NVVRVVALSG
GYSREDANDR LAQNHGLIAS FSRALSEGLS AQQSDDDFNN TLKHTIKAIY DASIT
//
