ID D1PFW5_9BACT Unreviewed; 376 AA.
AC D1PFW5;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Fructose-1,6-bisphosphate aldolase, class II {ECO:0000313|EMBL:EFB34404.1};
DE EC=4.1.2.13 {ECO:0000313|EMBL:EFB34404.1};
GN Name=fba {ECO:0000313|EMBL:EFB34404.1};
GN ORFNames=PREVCOP_06123 {ECO:0000313|EMBL:EFB34404.1};
OS Segatella copri DSM 18205.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=537011 {ECO:0000313|EMBL:EFB34404.1, ECO:0000313|Proteomes:UP000004477};
RN [1] {ECO:0000313|EMBL:EFB34404.1, ECO:0000313|Proteomes:UP000004477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18205 {ECO:0000313|EMBL:EFB34404.1,
RC ECO:0000313|Proteomes:UP000004477};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2009) 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:EFB34404.1}.
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DR EMBL; ACBX02000037; EFB34404.1; -; Genomic_DNA.
DR AlphaFoldDB; D1PFW5; -.
DR STRING; 537011.PREVCOP_06123; -.
DR PaxDb; 537011-PREVCOP_06123; -.
DR HOGENOM; CLU_040088_0_0_10; -.
DR Proteomes; UP000004477; 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 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 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:EFB34404.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000004477};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 134
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 135
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 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 230
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 274
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 376 AA; 41601 MW; 4C1F3C3FC1C33B69 CRC64;
MSQKKKVNLH SVRKEPHKFY TLLYIRKKNV SLNNKLSKIM AVDYKKIGLV NTKDMFARAI
KGGWAVPAFN FNNLEQLQAI IQASSNLKSP VILQVSKGAR KYANPTLLRY MAEGAVEYAK
ELGCNHPEIV LHLDHGDSFE TCKDCVDFGF SSVMIDGSAL PYEENIALTK KVVDYAHQFG
VTVEGELGVL AGVEDDVVAE ESHYTKPEEV VDFATRTGVD SLAISIGTSH GAYKFKPEQC
TRDPKTGHLV PPPLAFDVLA AVEEQLPGFP IVLHGSSSVP QEYVEIINKF GGKLPDAVGI
PEEQLTKASE SAVCKINIDS DSRLAFTAGV RETLALHPEY FDPRQYCGKA REYMVDLYSH
KIKDVLHSDN KLANLD
//
