ID B5EY54_SALA4 Unreviewed; 286 AA.
AC B5EY54;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Fructose-1,6-bisphosphate aldolase, class II {ECO:0000313|EMBL:ACH51832.1};
GN OrderedLocusNames=SeAg_B4006 {ECO:0000313|EMBL:ACH51832.1};
OS Salmonella agona (strain SL483).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166 {ECO:0000313|EMBL:ACH51832.1, ECO:0000313|Proteomes:UP000008819};
RN [1] {ECO:0000313|EMBL:ACH51832.1, ECO:0000313|Proteomes:UP000008819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483 {ECO:0000313|EMBL:ACH51832.1,
RC ECO:0000313|Proteomes:UP000008819};
RX PubMed=21602358; DOI=10.1128/JB.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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};
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DR EMBL; CP001138; ACH51832.1; -; Genomic_DNA.
DR RefSeq; WP_001131798.1; NC_011149.1.
DR AlphaFoldDB; B5EY54; -.
DR KEGG; sea:SeAg_B4006; -.
DR HOGENOM; CLU_040088_0_1_6; -.
DR Proteomes; UP000008819; Chromosome.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic 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 NCBIfam; TIGR00167; cbbA; 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.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 82
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 83
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 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 134
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 205
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"
SQ SEQUENCE 286 AA; 31355 MW; D60F04E34CD6490B CRC64;
MPLVNGRILL NCIQEKHVLA GAFNTTNLET TISILNAIER SGLPNFIQIA PTNAQLSGYD
YIYEIVKRHA DKMDIPVSLH LDHGKTLEDV KQAVRAGFTS VMIDGAALPF EENIAFTREA
VDFCKSFGVP VEAELGAILG KEDDHVSEAD CKTEPEKVQR FVEETGCDML AVSIGNVHGL
EDIPRIDIPL LQRIASVSPV PLVIHGGSGI DADILRSFVN YKVAKVNIAS DLRKAFITTV
GKAWVNNNNE ANLARVMANA KQAVEDDVYS KIKMMNKNHS AFRKVS
//
