ID V5T704_9LACO Unreviewed; 288 AA.
AC V5T704;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013779};
GN ORFNames=JG30_01660 {ECO:0000313|EMBL:KJY63255.1};
OS Bombilactobacillus mellifer.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Bombilactobacillus.
OX NCBI_TaxID=1218492 {ECO:0000313|EMBL:AHB59791.1};
RN [1] {ECO:0000313|EMBL:AHB59791.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bin4N {ECO:0000313|EMBL:AHB59791.1};
RX PubMed=24148670;
RA Butler E., Alsterfjord M., Olofsson T.C., Karlsson C., Malmstrom J.,
RA Vasquez A.;
RT "Proteins of novel lactic acid bacteria from Apis mellifera mellifera: an
RT insight into the production of known extra-cellular proteins during
RT microbial stress.";
RL BMC Microbiol. 13:235-235(2013).
RN [2] {ECO:0000313|EMBL:KJY63255.1, ECO:0000313|Proteomes:UP000033558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bin4 {ECO:0000313|EMBL:KJY63255.1,
RC ECO:0000313|Proteomes:UP000033558};
RA Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G.,
RA Vasquez A.;
RT "Comparative genomics of the lactic acid bacteria isolated from the honey
RT bee gut.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}.
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DR EMBL; KC776100; AHB59791.1; -; Genomic_DNA.
DR EMBL; JXJQ01000002; KJY63255.1; -; Genomic_DNA.
DR RefSeq; WP_046315351.1; NZ_KQ034028.1.
DR AlphaFoldDB; V5T704; -.
DR STRING; 1218492.JG30_01660; -.
DR PATRIC; fig|1218492.5.peg.279; -.
DR HOGENOM; CLU_040088_0_1_9; -.
DR OrthoDB; 9803995at2; -.
DR Proteomes; UP000033558; Unassembled WGS sequence.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:InterPro.
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; IPR011289; Fruc_bis_ald_class-2.
DR NCBIfam; TIGR00167; cbbA; 1.
DR NCBIfam; TIGR01859; fruc_bis_ald; 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 4: Predicted;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000033558};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 85
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 86
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 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 178
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 179
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 207
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 208..210
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 229..232
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ SEQUENCE 288 AA; 30720 MW; CA5A492D248DBC23 CRC64;
MALVNGNEIF KNARAGKYAV GAFNTNNLEW TRAILAAAEE TKTPILIQTS MGAAKYMGGY
ELCLHLVQDT VKSMGITVPV VMHLDHGNYE AAKECIKVGY NSVMFDGHDL PFAENLEKTK
EIVKLAHAQG MSVEAEVGSI GGTEDGITGA GELASVEEAQ TLAATGVDYL ACGIGNIHGV
YPANWQGLNF DRLQEIAAAV QTPLVLHGGS GIPKEQIVKA ISLGISKVNV NTECQLAFAK
ATRQYVEAGK DQDIDAKGYD PRKLLAPGTE AIKETVKERI AWFGTPAV
//
