ID F4LJI3_TREBD Unreviewed; 332 AA.
AC F4LJI3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Fructose-1,6-bisphosphate aldolase, class II {ECO:0000313|EMBL:AEE16378.1};
DE EC=4.1.2.13 {ECO:0000313|EMBL:AEE16378.1};
GN OrderedLocusNames=Trebr_0942 {ECO:0000313|EMBL:AEE16378.1};
OS Treponema brennaborense (strain DSM 12168 / CIP 105900 / DD5/3).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=906968 {ECO:0000313|EMBL:AEE16378.1, ECO:0000313|Proteomes:UP000006546};
RN [1] {ECO:0000313|Proteomes:UP000006546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12168 / CIP 105900 / DD5/3
RC {ECO:0000313|Proteomes:UP000006546};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I.,
RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Treponema brennaborense DSM 12168.";
RL Submitted (APR-2011) 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; CP002696; AEE16378.1; -; Genomic_DNA.
DR RefSeq; WP_013758097.1; NC_015500.1.
DR AlphaFoldDB; F4LJI3; -.
DR STRING; 906968.Trebr_0942; -.
DR KEGG; tbe:Trebr_0942; -.
DR eggNOG; COG0191; Bacteria.
DR HOGENOM; CLU_040088_0_0_12; -.
DR OrthoDB; 9803995at2; -.
DR Proteomes; UP000006546; Chromosome.
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.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:AEE16378.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000006546};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 93
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 94
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 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 191
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 234
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 332 AA; 36355 MW; DC9862CA618BCE8C CRC64;
MTSYKELGLV NTKELFAKAV KGGYAIPAYN FNNMEQLQAI IQACVETKSP VILQVSSGAR
KYANKNLLKN MARGAVEYAH ELGYDIPIVL HLDHGDTYEL CVDCIESGFS SVMIDGSSLP
YEENVALTKK VCEYAHSRAD YVTVEGELGV LAGVEDDVAA EESHYTKPEE VEDFVKRTGV
DSLAISIGTS HGRQKFKPEQ CTRTADGVLV PPPLAFDVLE AIEKKLPGFP IVLHGSSSVP
IEYVKEIEKY GGKLKDSVGI PEGQLRKAAK SAVCKINIDS DGRLAMTAAI RKVFSEHPEE
FDPRKYLGPA RDELKKLYMH KNKEVLGSAG NA
//
