ID E7N5B6_9FIRM Unreviewed; 294 AA.
AC E7N5B6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Ketose-bisphosphate aldolase {ECO:0000313|EMBL:EFW28608.1};
GN ORFNames=HMPREF9555_02211 {ECO:0000313|EMBL:EFW28608.1};
OS Selenomonas artemidis F0399.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=749551 {ECO:0000313|EMBL:EFW28608.1, ECO:0000313|Proteomes:UP000004633};
RN [1] {ECO:0000313|EMBL:EFW28608.1, ECO:0000313|Proteomes:UP000004633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0399 {ECO:0000313|EMBL:EFW28608.1,
RC ECO:0000313|Proteomes:UP000004633};
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., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) 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:EFW28608.1}.
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DR EMBL; AECV01000064; EFW28608.1; -; Genomic_DNA.
DR RefSeq; WP_009350858.1; NZ_GL638158.1.
DR AlphaFoldDB; E7N5B6; -.
DR STRING; 749551.HMPREF9555_02211; -.
DR HOGENOM; CLU_040088_0_1_9; -.
DR Proteomes; UP000004633; Unassembled WGS sequence.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
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 Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
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 189
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
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 294 AA; 31801 MW; 78D2BD06D61BF2F3 CRC64;
MPLVNMKKML ADARRGKYAI GAFDVSNFDM AAAVTETARE ERSPVILMGL TPDLADGKLP
YWLDSVKALA AAADVPVAVH LDHATDLDFI KECVDGGFSS VMFDGSLLPL EENIRKTREV
VAYAHRFDVT VEAELGHVGD GIVGSSEIGA EKKTGFDNPD DFLTQPDELA DFIARTEADC
IAVAVGTAHG LYVREPKLHF DRLAALNDIS PVPMVMHGGS GTPDDQIRKA VALGICKLNI
FSEMLTAFNG ALKEELAHAE HLAIWPHQLY QKPLAALREV VRRKITLVGS AGKA
//
