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Database: UniProt
Entry: F8X0N9_9BACT
LinkDB: F8X0N9_9BACT
Original site: F8X0N9_9BACT 
ID   F8X0N9_9BACT            Unreviewed;       332 AA.
AC   F8X0N9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Fructose-bisphosphate aldolase {ECO:0000313|EMBL:EGK03591.1};
GN   ORFNames=HMPREF9456_01658 {ECO:0000313|EMBL:EGK03591.1};
OS   Dysgonomonas mossii DSM 22836.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC   Dysgonomonas.
OX   NCBI_TaxID=742767 {ECO:0000313|EMBL:EGK03591.1, ECO:0000313|Proteomes:UP000006420};
RN   [1] {ECO:0000313|EMBL:EGK03591.1, ECO:0000313|Proteomes:UP000006420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22836 {ECO:0000313|EMBL:EGK03591.1,
RC   ECO:0000313|Proteomes:UP000006420};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Pudlo N., Martens E.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Dysgonomonas mossii DSM 22836.";
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};
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:EGK03591.1}.
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DR   EMBL; ADLW01000006; EGK03591.1; -; Genomic_DNA.
DR   RefSeq; WP_006843029.1; NZ_GL892006.1.
DR   AlphaFoldDB; F8X0N9; -.
DR   STRING; 742767.HMPREF9456_01658; -.
DR   GeneID; 78082310; -.
DR   eggNOG; COG0191; Bacteria.
DR   HOGENOM; CLU_040088_0_0_10; -.
DR   OrthoDB; 9803995at2; -.
DR   Proteomes; UP000006420; Unassembled WGS sequence.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
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   Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006420};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT   ACT_SITE        94
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT   BINDING         95
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         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         190
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         233
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;  36196 MW;  C6F0027499549A68 CRC64;
     MVSYKDLGLV NTKEMFAKAV KGGYAIPAFN VNNMEQLQAI VQAASETKSP VIVQASKGAR
     QYANPILLRY MLQGAVEYAK SLGWEKPQIV LHLDHGDTFE TCKDCIDSGF SSVMIDGSHL
     PYEENIALTK KVVEYAHQFG VTVEGELGVL AGVEDEVVAE HHTYTRPEEV VDFATRTGCD
     SLAISIGTSH GANKFTPEQC TRDEKGHLVP PPLRFDILEA IEKELPGFPI VLHGASSVPQ
     EEVATINKYG GALKDAIGIP EEQLRRAAKS AVCKINIDSD SRLALTAAVR EVFATKPAEF
     DPRKYLGPAR DNMKKLYKHK IEAVLGSAGK AE
//
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