ID A0A0A6Y2G8_9FLAO Unreviewed; 296 AA. AC A0A0A6Y2G8; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 22-FEB-2023, entry version 34. 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=HMPREF9074_08244 {ECO:0000313|EMBL:KHE69690.1}; OS Capnocytophaga sp. oral taxon 329 str. F0087. OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=706436 {ECO:0000313|EMBL:KHE69690.1, ECO:0000313|Proteomes:UP000030579}; RN [1] {ECO:0000313|EMBL:KHE69690.1, ECO:0000313|Proteomes:UP000030579} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0087 {ECO:0000313|EMBL:KHE69690.1, RC ECO:0000313|Proteomes:UP000030579}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L., RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C., RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A., RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W., RA Chinwalla A., Mardis E.R., Wilson R.K.; RL Submitted (OCT-2014) 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:KHE69690.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AFHP02000095; KHE69690.1; -; Genomic_DNA. DR RefSeq; WP_009390883.1; NZ_KN390002.1. DR AlphaFoldDB; A0A0A6Y2G8; -. DR STRING; 706436.HMPREF9074_08244; -. DR EnsemblBacteria; KHE69690; KHE69690; HMPREF9074_08244. DR eggNOG; COG3588; Bacteria. DR HOGENOM; CLU_081560_0_0_10; -. DR OrthoDB; 9813469at2; -. DR UniPathway; UPA00109; UER00183. DR Proteomes; UP000030579; 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|HAMAP-Rule:MF_00729}; KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00729}. FT ACT_SITE 177 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00729" FT ACT_SITE 214 FT /note="Schiff-base intermediate with dihydroxyacetone-P" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00729" SQ SEQUENCE 296 AA; 33215 MW; FECCA02DB35E0B5C CRC64; MKKEQLEQMK NGKGFIAALD QSGGSTPKAL KLYGIDESQY TNDAEMFALI HQMRTRIIKS PAFNSEKILG AILFEQTMDN LIDGKYTADY LWEEKHIIPF LKVDKGLLDI DSDGVQLMKP IDGLPDLLKR ANERHIFGTK MRSVIKEASP RGIAQVVAQQ FEVAQVIIDA GLVPIIEPEV DITIPDKSRA EAILRDEIRK HLDRLRDTSD VMLKLSLPTI DNFYKEFTKH PRVVRVVALS GGYPREKANE ILAKNKGVIA SFSRALTQGL SAQQTDTEFN QMLAETIEGI YEASVK //