ID A0A4Z0F0G7_BRUSS Unreviewed; 354 AA. AC A0A4Z0F0G7; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 16-OCT-2019, entry version 2. 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|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 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|RuleBase:RU365019}; KW Zinc {ECO:0000256|RuleBase:RU365019}. 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 //