ID A0A0J1EZA8_9MICC Unreviewed; 286 AA.
AC A0A0J1EZA8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Fructose-bisphosphate aldolase {ECO:0000313|EMBL:KLU10749.1};
GN ORFNames=ABL57_04595 {ECO:0000313|EMBL:KLU10749.1};
OS Kocuria sp. SM24M-10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=1660349 {ECO:0000313|EMBL:KLU10749.1, ECO:0000313|Proteomes:UP000036489};
RN [1] {ECO:0000313|EMBL:KLU10749.1, ECO:0000313|Proteomes:UP000036489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM24M-10 {ECO:0000313|EMBL:KLU10749.1,
RC ECO:0000313|Proteomes:UP000036489};
RA Palermo B.R., Castro D.B., Cauz A.C., Magalhaes B.L., Carlos C.,
RA Costa F.L., Scagion G.P., Higac J.H., Pereira L.B., Almeida L.D.,
RA Neves M.S., Cordeiro M.A., Prado P.F., Silva T.M., Balsalobre T.W.,
RA Paulino L.C., Vicentini R., Ferraz L.F., Ottoboni L.M.;
RT "Draft genome sequence of Kocuria sp. SM24M-10 isolated from coral mucus.";
RL Submitted (MAY-2015) 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:KLU10749.1}.
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DR EMBL; LDNX01000043; KLU10749.1; -; Genomic_DNA.
DR RefSeq; WP_047802275.1; NZ_LDNX01000043.1.
DR AlphaFoldDB; A0A0J1EZA8; -.
DR PATRIC; fig|1660349.3.peg.2926; -.
DR OrthoDB; 9803995at2; -.
DR Proteomes; UP000036489; 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 Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43060:SF17; L-THREONATE DEHYDROGENASE; 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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 81
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 82
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 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 132
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 178
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 206
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 207..209
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 228..231
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ SEQUENCE 286 AA; 29598 MW; 5D5934D377C4908C CRC64;
MRANLLDVVT SALAAHTAVP ALSTYDFTTA QAVVEASERA GRPVILLVPP KAAAGTGGRR
LVTALRALAD DAATPVCVQL DHAVDLDLIE HAVAAGADAV LADGSALPAA ANAAFVARAR
ELVGPGVVVE AELGSLPGDE DAAMTSEAGG MTDPGEVPGF LDGSGADLLA VAVGNVHGHY
RGTPRLHWSR LEQICEAAER TPLVLHGASG IPETMLVRAP LAGIGKININ TELRSAVFAA
VADRIEQRRH QGLSLWALLE DWTEAVGEFT TLAHRLTTAE ARSRNS
//
