ID A0A4Z0F0G7_BRUSS Unreviewed; 354 AA. AC A0A4Z0F0G7; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 13-NOV-2019, entry version 3. 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; OC Brucellaceae; 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 RT by 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- CC phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in CC gluconeogenesis and the reverse reaction in glycolysis. CC {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; CC EC=4.1.2.13; 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 CC other provides a structural contribution. CC {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 CC contribution. {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 CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 UniPathway; UPA00109; UER00183. DR Proteomes; UP000297495; Unassembled WGS sequence. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW. 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 Complete proteome {ECO:0000313|Proteomes:UP000297495}; 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 Dihydroxyacetone phosphate binding. FT {ECO:0000256|PIRSR:PIRSR001359-2}. FT REGION 275 278 Dihydroxyacetone phosphate binding. FT {ECO:0000256|PIRSR:PIRSR001359-2}. FT ACT_SITE 83 83 Proton donor. {ECO:0000256|PIRSR: FT PIRSR001359-1}. FT METAL 84 84 Zinc 1; catalytic. {ECO:0000256|PIRSR: FT PIRSR001359-3}. FT METAL 105 105 Zinc 2. {ECO:0000256|PIRSR:PIRSR001359- FT 3}. FT METAL 142 142 Zinc 2. {ECO:0000256|PIRSR:PIRSR001359- FT 3}. FT METAL 198 198 Zinc 1; catalytic. {ECO:0000256|PIRSR: FT PIRSR001359-3}. FT METAL 232 232 Zinc 1; catalytic. {ECO:0000256|PIRSR: FT PIRSR001359-3}. FT BINDING 199 199 Dihydroxyacetone phosphate; via amide FT nitrogen. {ECO:0000256|PIRSR:PIRSR001359- FT 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 //