ID A0A084JCC2_9CLOT Unreviewed; 315 AA.
AC A0A084JCC2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Class II fructose-1,6-bisphosphate aldolase {ECO:0000313|EMBL:MBE6059906.1};
DE EC=4.1.2.13 {ECO:0000313|EMBL:KEZ86606.1, ECO:0000313|EMBL:MBE6059906.1};
DE SubName: Full=Fructose-bisphosphate aldolase {ECO:0000313|EMBL:KEZ86606.1};
GN Name=fba {ECO:0000313|EMBL:MBE6059906.1};
GN ORFNames=E7215_07000 {ECO:0000313|EMBL:MBE6059906.1}, IO99_08990
GN {ECO:0000313|EMBL:KEZ86606.1};
OS Clostridium sulfidigenes.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=318464 {ECO:0000313|EMBL:KEZ86606.1, ECO:0000313|Proteomes:UP000028542};
RN [1] {ECO:0000313|EMBL:KEZ86606.1, ECO:0000313|Proteomes:UP000028542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=113A {ECO:0000313|EMBL:KEZ86606.1,
RC ECO:0000313|Proteomes:UP000028542};
RA Honkalas V.S., Dabir A.P., Arora P., Dhakephalkar P.K.;
RT "Draft genome of Clostridium sulfidigenes 113A isolated from sediments
RT associated with methane hydrate from Krishna Godavari basin.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBE6059906.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SIG254 {ECO:0000313|EMBL:MBE6059906.1};
RA Peng X.;
RT "Evolution of Biomass-Degrading Anaerobic Consortia Revealed by
RT Metagenomics.";
RL Submitted (APR-2019) 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 -!- 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:KEZ86606.1}.
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DR EMBL; JPMD01000020; KEZ86606.1; -; Genomic_DNA.
DR EMBL; SVCM01000077; MBE6059906.1; -; Genomic_DNA.
DR RefSeq; WP_035132444.1; NZ_JPMD01000020.1.
DR AlphaFoldDB; A0A084JCC2; -.
DR STRING; 318464.IO99_08990; -.
DR GeneID; 84601160; -.
DR eggNOG; COG0191; Bacteria.
DR Proteomes; UP000028542; Unassembled WGS sequence.
DR Proteomes; UP000768462; 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: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.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:KEZ86606.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000028542};
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 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 216
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 217..219
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 259..262
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ SEQUENCE 315 AA; 34498 MW; 550A8BA67AA1BE15 CRC64;
MALVTTKEMF KKAFEGKYAI GAFNINNMEI IQGIVDGAKA QNSAVILQCS SGAIKYMRPA
YLRHMVLAAV EESGVDVALH LDHGDSFELC KECIDNGFTS VMFDGSHYDY EENVRLTKEV
VEYAHAHGVV VEAELGKLAG VEDDVNVSAK DATYTDPDQA VDFVKRTGVD SLAIAIGTSH
GAYKFKGEAK LDFERLETIT RKLEEVGFEK YPIVLHGASA VDPKYVEMCN ENGGDIKGAK
GVPVEMLRKA SSMAVCKINM DTDLRLCVTG SCRKVFADKP SEFDPRKYLG VARTNLQQLV
EDKITTVLGS IDSMK
//
