ID B3CEM7_9BACE Unreviewed; 334 AA.
AC B3CEM7;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Fructose-1,6-bisphosphate aldolase, class II {ECO:0000313|EMBL:EDV05015.1};
DE EC=4.1.2.13 {ECO:0000313|EMBL:EDV05015.1};
GN Name=fba {ECO:0000313|EMBL:EDV05015.1};
GN ORFNames=BACINT_04158 {ECO:0000313|EMBL:EDV05015.1};
OS Bacteroides intestinalis DSM 17393.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=471870 {ECO:0000313|EMBL:EDV05015.1, ECO:0000313|Proteomes:UP000004596};
RN [1] {ECO:0000313|EMBL:EDV05015.1, ECO:0000313|Proteomes:UP000004596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV05015.1,
RC ECO:0000313|Proteomes:UP000004596};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides intestinalis (DSM 17393).";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDV05015.1, ECO:0000313|Proteomes:UP000004596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV05015.1,
RC ECO:0000313|Proteomes:UP000004596};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2008) 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:EDV05015.1}.
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DR EMBL; ABJL02000008; EDV05015.1; -; Genomic_DNA.
DR RefSeq; WP_007212863.1; NZ_ABJL02000008.1.
DR AlphaFoldDB; B3CEM7; -.
DR STRING; 471870.BACINT_04158; -.
DR GeneID; 69507286; -.
DR eggNOG; COG0191; Bacteria.
DR OrthoDB; 9803995at2; -.
DR Proteomes; UP000004596; 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:EDV05015.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
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 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 334 AA; 36677 MW; 2761B67843BFAE9C CRC64;
MINYKDLGLV NTREMFAKAI KGGYAIPAFN FNNMEQLQAI VKAAVETKSP VILQVSKGAR
QYANQTLLRY MAEGAVEYAK ELGCKHPEIV LHLDHGDTFE TCKSCIDMGF SSVMIDGSHL
PYEENVALTK KVVDYAHQFD VTVEGELGVL AGVEDEVSAE HHTYTDPEEV IDFATRTGCD
SLAISIGTSH GAYKFKPEQC HVDPKTGRLV PPPLAFEVLD AVMEKLPGFP IVLHGSSSVP
QEEVETINKF GGKLEAAIGI PEEELRKAAK SAVCKINIDS DSRLAMTAAI RKVFAEKPAE
FDPRKYLGPA RDNMEKMYMH KIINVLGSDG KLAE
//
