ID A0A4Z0F0G7_BRUSS Unreviewed; 354 AA. AC A0A4Z0F0G7; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 11-DEC-2019, entry version 4. DE RecName: Full=Fructose-1,6-bisphosphate aldolase {ECO:0000256|RuleBase:RU365019}; DE Short=FBP aldolase {ECO:0000256|RuleBase:RU365019}; DE EC=4.1.2.13 {ECO:0000256|RuleBase:RU365019}; GN ORFNames=E4658_08295 {ECO:0000313|EMBL:TFZ71086.1}; OS Brucella suis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Brucellaceae; OC Brucella. OX NCBI_TaxID=29461 {ECO:0000313|EMBL:TFZ71086.1, ECO:0000313|Proteomes:UP000297495}; RN [1] {ECO:0000313|EMBL:TFZ71086.1, ECO:0000313|Proteomes:UP000297495} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bw_180660 {ECO:0000313|EMBL:TFZ71086.1, RC ECO:0000313|Proteomes:UP000297495}; RA Zange S., Schneider K., Georgi E., Scholz H.C., Antwerpen M.H., RA Walter M.C., Zoeller L., Von Buttlar H., Borde J.P.; RT "A headache with surprising outcome: First case of brucellosis caused by RT Brucella suis biovar 1 in Germany."; RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone CC phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate CC (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and CC the reverse reaction in glycolysis. {ECO:0000256|RuleBase:RU365019}. 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|RuleBase:RU365019}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR001359-3}; CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other CC provides a structural contribution. {ECO:0000256|PIRSR:PIRSR001359-3}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU365019}; CC Note=One is catalytic and the other provides a structural contribution. CC {ECO:0000256|RuleBase:RU365019}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC {ECO:0000256|RuleBase:RU365019}. CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase CC family. {ECO:0000256|RuleBase:RU365019}. 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:TFZ71086.1}. 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; SRIH01000022; TFZ71086.1; -; Genomic_DNA. DR RefSeq; WP_004689104.1; NZ_UFTY01000002.1. DR KEGG; bsg:IY72_15300; -. DR KEGG; bsw:IY71_15350; -. DR KO; K01624; -. DR UniPathway; UPA00109; UER00183. DR Proteomes; UP000297495; Unassembled WGS sequence. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR CDD; cd00947; TBP_aldolase_IIB; 1. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000771; FBA_II. DR InterPro; IPR006412; Fruct_bisP_Calv. DR Pfam; PF01116; F_bP_aldolase; 1. DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1. DR TIGRFAMs; TIGR00167; cbbA; 1. DR TIGRFAMs; TIGR01521; FruBisAldo_II_B; 1. DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1. DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1. PE 3: Inferred from homology; KW Glycolysis {ECO:0000256|RuleBase:RU365019}; KW Lyase {ECO:0000256|RuleBase:RU365019}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3, KW ECO:0000256|RuleBase:RU365019}; KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3, ECO:0000256|RuleBase:RU365019}. FT REGION 233..235 FT /note="Dihydroxyacetone phosphate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2" FT REGION 275..278 FT /note="Dihydroxyacetone phosphate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2" FT ACT_SITE 83 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1" FT METAL 84 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT METAL 105 FT /note="Zinc 2" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT METAL 142 FT /note="Zinc 2" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT METAL 198 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT METAL 232 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3" FT BINDING 199 FT /note="Dihydroxyacetone phosphate; via amide nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2" SQ SEQUENCE 354 AA; 38787 MW; 90E72421F0D9FD2B CRC64; MARITLRQLL DHAAEKGYGV PAFNINNMEQ ALAIMEAANA VDAPVILQAS RGARSYANDI MLRHMMDAVT EIYPHIPVCV HLDHGNEAAT CMSAIQAGFT SVMMDGSLKA DGKTPADWDY NVSVTRQVSE MSHLGGISVE GELGVLGSLE TGMGDAEDGH GAEGKLSHDQ LLTDPDEAVK FVRETKVDAL AIAMGTSHGA YKFSRKPDGS VLAMHVIEEI HRKLPNTHLV MHGSSSVPEE LQEIINKYGG QMKPTWGVPV EEIQRGIKHG VRKINIDTDN RMAMTGQIRR ILQEEPSEFD PRKYLKPAMA AMTKLCKERF EQFGTAGHAA SIRPIPLSEM AKRYRDGSLD PKFS //