ID A0A0J8VEX7_9GAMM Unreviewed; 284 AA.
AC A0A0J8VEX7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=tagatose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00012905};
DE EC=4.1.2.40 {ECO:0000256|ARBA:ARBA00012905};
DE AltName: Full=D-tagatose-bisphosphate aldolase class II {ECO:0000256|ARBA:ARBA00032933};
DE AltName: Full=Tagatose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00031246};
GN ORFNames=C9I94_07370 {ECO:0000313|EMBL:PSW25463.1};
OS Photobacterium swingsii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=680026 {ECO:0000313|EMBL:PSW25463.1, ECO:0000313|Proteomes:UP000240481};
RN [1] {ECO:0000313|EMBL:PSW25463.1, ECO:0000313|Proteomes:UP000240481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24669 {ECO:0000313|EMBL:PSW25463.1,
RC ECO:0000313|Proteomes:UP000240481};
RA Butler K.;
RT "Whole genome sequencing of Histamine producing bacteria.";
RL Submitted (JAN-2018) 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 metabolism; D-tagatose 6-phosphate degradation;
CC D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-
CC phosphate: step 2/2. {ECO:0000256|ARBA:ARBA00005191}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSW25463.1}.
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DR EMBL; PYLZ01000003; PSW25463.1; -; Genomic_DNA.
DR RefSeq; WP_048897505.1; NZ_PYLZ01000003.1.
DR AlphaFoldDB; A0A0J8VEX7; -.
DR STRING; 680026.AB733_03455; -.
DR OrthoDB; 9803995at2; -.
DR UniPathway; UPA00704; UER00716.
DR Proteomes; UP000240481; Unassembled WGS sequence.
DR GO; GO:0009025; F:tagatose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:2001059; P:D-tagatose 6-phosphate catabolic 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; IPR011288; TagBP_ald_KbaY/GatY.
DR NCBIfam; TIGR00167; cbbA; 1.
DR NCBIfam; TIGR01858; tag_bisphos_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 Zinc {ECO:0000256|ARBA:ARBA00022833, 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 180
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 181
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 208
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 209..211
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 230..233
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ SEQUENCE 284 AA; 31211 MW; 227810F2A8296229 CRC64;
MFLVSSREML HKAQLGGYAV PAFNIHNLET VQVVVETAAE MRSPVILAGT PGTFSYAGTD
YLVGICKEAA KRYEMPIALH LDHHESYTDI RQKIEAGIKS AMIDGSHLPF EENIELVKKV
VAFCHRWDCS VEAELGRLGG QEDDLIVDSK DALFTDPDNA IEFIEKTGID SLAIAIGTAH
GMYKEEPCLD FDRLGIIRSK TDVPLVLHGA SGVPDQDVRR CIELGITKVN VATELKIAFS
DAVKQYFLDN PSANDPRHYI VPGKAAMKQV VIDKIRVCGS EGKL
//
