ID A7BBV8_9ACTO Unreviewed; 282 AA.
AC A7BBV8;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE SubName: Full=Ketose-bisphosphate aldolase {ECO:0000313|EMBL:EDN80682.1};
GN ORFNames=ACTODO_01129 {ECO:0000313|EMBL:EDN80682.1};
OS Schaalia odontolytica ATCC 17982.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=411466 {ECO:0000313|EMBL:EDN80682.1, ECO:0000313|Proteomes:UP000003553};
RN [1] {ECO:0000313|EMBL:EDN80682.1, ECO:0000313|Proteomes:UP000003553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17982 {ECO:0000313|EMBL:EDN80682.1,
RC ECO:0000313|Proteomes:UP000003553};
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-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDN80682.1, ECO:0000313|Proteomes:UP000003553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17982 {ECO:0000313|EMBL:EDN80682.1,
RC ECO:0000313|Proteomes:UP000003553};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Actinomyces odontolyticus (ATCC 17982).";
RL Submitted (MAY-2007) 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:EDN80682.1}.
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DR EMBL; AAYI02000004; EDN80682.1; -; Genomic_DNA.
DR RefSeq; WP_003792218.1; NZ_DS264586.1.
DR AlphaFoldDB; A7BBV8; -.
DR eggNOG; COG0191; Bacteria.
DR HOGENOM; CLU_040088_0_1_11; -.
DR Proteomes; UP000003553; 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 83
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 84
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 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 177
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 205
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 282 AA; 29530 MW; 6AFE87FC5BFF4890 CRC64;
MLADTAELAR DAAQRGQGLA AFNVVLLDHA EAFIDAAQEA QLPLVLQLSQ NAVAYHGGRL
APIGRALIEL ASEATVPVSV HLDHAESTDL CRAAVDLGFT SIMYDGSVLP DDVNRATTAA
MVEMAHASGV SVEAELGEVG GKNGVHDPKA RTKPEDAAQF VADTGVDLLA VAVGSSHAMA
TRDAVLDTEL IAAIKRAVPV PLVLHGSSGV PDDGMVAAIN AGMTKINVST HLNVVFTSRI
RDILLHDPGL VDPRKYVGPA TGIVRDEVRR LMELYAPWCA VA
//
