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Database: UniProt
Entry: I7IL75_9BURK
LinkDB: I7IL75_9BURK
Original site: I7IL75_9BURK 
ID   I7IL75_9BURK            Unreviewed;       354 AA.
AC   I7IL75;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
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   Name=fba {ECO:0000313|EMBL:CCG19849.1};
GN   ORFNames=KUM_1064 {ECO:0000313|EMBL:CCG19849.1};
OS   Taylorella asinigenitalis 14/45.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Taylorella.
OX   NCBI_TaxID=1091495 {ECO:0000313|EMBL:CCG19849.1};
RN   [1] {ECO:0000313|EMBL:CCG19849.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=14/45 {ECO:0000313|EMBL:CCG19849.1};
RX   PubMed=22541164; DOI=10.1016/j.vetmic.2012.03.041;
RA   Hauser H., Richter D.C., van Tonder A., Clark L., Preston A.;
RT   "Comparative genomic analyses of the Taylorellae.";
RL   Vet. Microbiol. 159:195-203(2012).
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|ARBA:ARBA00002181,
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; EC=4.1.2.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00000441,
CC         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|ARBA:ARBA00004714, ECO:0000256|RuleBase:RU365019}.
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. {ECO:0000256|RuleBase:RU365019}.
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DR   EMBL; HE681424; CCG19849.1; -; Genomic_DNA.
DR   RefSeq; WP_014111961.1; NC_021033.1.
DR   AlphaFoldDB; I7IL75; -.
DR   KEGG; tat:KUM_1064; -.
DR   HOGENOM; CLU_040088_0_0_4; -.
DR   UniPathway; UPA00109; UER00183.
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; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000771; FBA_II.
DR   InterPro; IPR006412; Fruct_bisP_Calv.
DR   NCBIfam; TIGR00167; cbbA; 1.
DR   NCBIfam; TIGR01521; FruBisAldo_II_B; 1.
DR   PANTHER; PTHR30304; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR30304:SF0; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE SUBUNIT GATY-RELATED; 1.
DR   Pfam; PF01116; F_bP_aldolase; 1.
DR   PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR   SUPFAM; SSF51569; Aldolase; 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, ECO:0000313|EMBL:CCG19849.1};
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   ACT_SITE        83
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         198
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         199
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT   BINDING         232
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         233..235
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT   BINDING         275..278
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ   SEQUENCE   354 AA;  38823 MW;  4BC4F68F8AE8FCC7 CRC64;
     MALVSLRQLL DHAAEFGYGI PAFNVNNLEQ VQAIMEAARE TDSPVIMQAS AGARKYAGEP
     FLKHLIQAAV EAYPDIPIVM HQDHGQSPDV CRGAINLGFT SVMMDGSLMP DGKTIATYEY
     NVQTTREVVQ MAHAIGVSVE GELGVLGSLE TMKGDKEDGH GAEGTLTRDQ LLTDPEQAAE
     FVRETQVDAL AIAIGTSHGA YKFTRKPTGD ILSIQRIKEI NARLPNTHIV MHGSSSVPQE
     YLEQIRMYGG DMRETYGVPV EEIQEAIKYG VRKVNIDTDI RLAMTAAVRK FLHENPSKFD
     PREFNKPARE AAKQLCISRY EAFGTAGNAS KIKPVELSTM AQKYASGELV QKVN
//
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