ID A0A174FH79_9CLOT Unreviewed; 383 AA.
AC A0A174FH79;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Class II fructose-bisphosphate aldolase {ECO:0000313|EMBL:RGD72137.1};
DE SubName: Full=Fructose/tagatose bisphosphate aldolase {ECO:0000313|EMBL:CUO47475.1};
DE EC=4.1.2.13 {ECO:0000313|EMBL:CUO47475.1};
GN Name=Fba {ECO:0000313|EMBL:CUO47475.1};
GN ORFNames=DWX31_03635 {ECO:0000313|EMBL:RGD72137.1}, DXC39_10600
GN {ECO:0000313|EMBL:RGM05846.1}, DXD79_24220
GN {ECO:0000313|EMBL:RGI99165.1}, ERS852407_02922
GN {ECO:0000313|EMBL:CUO47475.1};
OS Hungatella hathewayi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX NCBI_TaxID=154046 {ECO:0000313|EMBL:CUO47475.1, ECO:0000313|Proteomes:UP000095651};
RN [1] {ECO:0000313|EMBL:CUO47475.1, ECO:0000313|Proteomes:UP000095651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608850 {ECO:0000313|EMBL:CUO47475.1,
RC ECO:0000313|Proteomes:UP000095651};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000261023, ECO:0000313|Proteomes:UP000261257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF19-13AC {ECO:0000313|EMBL:RGD72137.1,
RC ECO:0000313|Proteomes:UP000261023}, TF05-11AC
RC {ECO:0000313|EMBL:RGM05846.1, ECO:0000313|Proteomes:UP000261257}, and
RC TM09-12 {ECO:0000313|EMBL:RGI99165.1,
RC ECO:0000313|Proteomes:UP000263014};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-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};
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DR EMBL; CYZE01000007; CUO47475.1; -; Genomic_DNA.
DR EMBL; QTJW01000002; RGD72137.1; -; Genomic_DNA.
DR EMBL; QSON01000014; RGI99165.1; -; Genomic_DNA.
DR EMBL; QSSQ01000006; RGM05846.1; -; Genomic_DNA.
DR RefSeq; WP_002600860.1; NZ_QTJW01000002.1.
DR AlphaFoldDB; A0A174FH79; -.
DR OrthoDB; 9803995at2; -.
DR Proteomes; UP000095651; Unassembled WGS sequence.
DR Proteomes; UP000261023; Unassembled WGS sequence.
DR Proteomes; UP000261257; Unassembled WGS sequence.
DR Proteomes; UP000263014; Unassembled WGS sequence.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:CUO47475.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000095651};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 98
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 99
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 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 194
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 195
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 228
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 229..231
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 271..274
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ SEQUENCE 383 AA; 41434 MW; 5F6761985696C8D3 CRC64;
MPLIPLRPLM EATIKYGFGQ GAFNVNAVAQ AKAAIEVHEM FRSPAILQGA DLANGFMGGR
TDFMNATLED KKIGAKNIAD AVKKYGADSD IPIVLHLDHG RDFDSCVAAI EGGYTSVMID
GSSLPFDENV DLTREVVKYA HARGVSVEGE LGVLAGVEDH VFSASSTYTN PLKAVEFFRK
TGVDALAISY GTMHGASKGK DVKLRKEIAT AIRECLSHEG IFGALVSHGS STVPKYIVDE
INALGGELTN AYGISIEELQ AAIPCGINKI NVDTDIRLAV TRNMKELFVK YPELRTSASI
GEIYELLEAK KSQFDPRVFL PPIMDTVMKG TIPDDDVAAI VNCVERGVKE VVGTLIVQFG
SFGKAPLVEQ VTLEEMIERY KKN
//
