ID R8WN08_9ENTR Unreviewed; 284 AA.
AC R8WN08;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=D-tagatose-1,6-bisphosphate aldolase subunit GatY {ECO:0000256|HAMAP-Rule:MF_01294};
DE Short=TBPA {ECO:0000256|HAMAP-Rule:MF_01294};
DE Short=TagBP aldolase {ECO:0000256|HAMAP-Rule:MF_01294};
DE EC=4.1.2.40 {ECO:0000256|HAMAP-Rule:MF_01294};
DE AltName: Full=D-tagatose-bisphosphate aldolase class II {ECO:0000256|HAMAP-Rule:MF_01294};
DE AltName: Full=Tagatose-bisphosphate aldolase {ECO:0000256|HAMAP-Rule:MF_01294};
GN Name=gatY {ECO:0000256|HAMAP-Rule:MF_01294};
GN ORFNames=WC7_03983 {ECO:0000313|EMBL:EOQ45951.1};
OS Citrobacter sp. KTE151.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=1169322 {ECO:0000313|EMBL:EOQ45951.1, ECO:0000313|Proteomes:UP000014006};
RN [1] {ECO:0000313|EMBL:EOQ45951.1, ECO:0000313|Proteomes:UP000014006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTE151 {ECO:0000313|EMBL:EOQ45951.1,
RC ECO:0000313|Proteomes:UP000014006};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Nielsen K.L., Frimodt-Moller N., Andersen P.S., Walker B.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Escherichia coli KTE151.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of the tagatose-1,6-bisphosphate aldolase
CC GatYZ, which catalyzes the reversible aldol condensation of
CC dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with
CC glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate
CC (TBP). Requires GatZ subunit for full activity and stability. Is
CC involved in the catabolism of galactitol. {ECO:0000256|HAMAP-
CC Rule:MF_01294}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-tagatofuranose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:22948,
CC ChEBI:CHEBI:57642, ChEBI:CHEBI:58694, ChEBI:CHEBI:59776; EC=4.1.2.40;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01294};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01294};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01294};
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, ECO:0000256|HAMAP-
CC Rule:MF_01294}.
CC -!- SUBUNIT: Forms a complex with GatZ. {ECO:0000256|HAMAP-Rule:MF_01294}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. TagBP aldolase GatY subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01294}.
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:EOQ45951.1}.
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DR EMBL; ASQK01000011; EOQ45951.1; -; Genomic_DNA.
DR RefSeq; WP_016154640.1; NZ_KB976065.1.
DR AlphaFoldDB; R8WN08; -.
DR PATRIC; fig|1169322.3.peg.3988; -.
DR HOGENOM; CLU_040088_0_1_6; -.
DR UniPathway; UPA00704; UER00716.
DR Proteomes; UP000014006; Unassembled WGS sequence.
DR GO; GO:0009025; F:tagatose-bisphosphate aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:2001059; P:D-tagatose 6-phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019404; P:galactitol catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00947; TBP_aldolase_IIB; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_01294; TagBP_aldolase_GatY; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR011288; TagBP_ald_KbaY/GatY.
DR InterPro; IPR023955; TagBP_aldolase_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.
PE 3: Inferred from homology;
KW Galactitol metabolism {ECO:0000256|ARBA:ARBA00022877, ECO:0000256|HAMAP-
KW Rule:MF_01294}; Lyase {ECO:0000256|HAMAP-Rule:MF_01294};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01294,
KW ECO:0000256|PIRSR:PIRSR001359-3};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01294}.
FT ACT_SITE 82
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01294,
FT ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01294"
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 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01294"
FT BINDING 181
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01294,
FT ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01294"
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|HAMAP-Rule:MF_01294,
FT ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 230..233
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01294,
FT ECO:0000256|PIRSR:PIRSR001359-2"
SQ SEQUENCE 284 AA; 30876 MW; F7FBB4CE5207CED3 CRC64;
MFIISSKNML QKAQRDGYAV PAFNIHNLET LQVVVETAAE MRSPLIVAGT PGTFSYAGTG
NIVAIAGDLA REHNLPLAIH LDHHESTVDI ESKVLAGIRS VMIDGSHFPF EENVVLVKKV
VDFCHRYDTS AEAELGRLGG VEDDLIVDSK DALYTNPQQA REFVARTGID SLAVAIGTAH
GLYAAEPKLD FNRLAEIRAQ VDIPLVLHGA SGLPENDIRK AISLGVCKVN VATELKIAFS
DALKQYFAQN PKANDPRHYM QPAKQAMKAV VRKVIHVCGC EGQL
//
