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Database: UniProt
Entry: A0A0T2L0C5_9MICO
LinkDB: A0A0T2L0C5_9MICO
Original site: A0A0T2L0C5_9MICO 
ID   A0A0T2L0C5_9MICO        Unreviewed;       286 AA.
AC   A0A0T2L0C5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Ketose-bisphosphate aldolase {ECO:0000313|EMBL:KRA25306.1};
GN   ORFNames=ASD65_13400 {ECO:0000313|EMBL:KRA25306.1};
OS   Microbacterium sp. Root61.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA25306.1, ECO:0000313|Proteomes:UP000051216};
RN   [1] {ECO:0000313|EMBL:KRA25306.1, ECO:0000313|Proteomes:UP000051216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root61 {ECO:0000313|EMBL:KRA25306.1,
RC   ECO:0000313|Proteomes:UP000051216};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA25306.1, ECO:0000313|Proteomes:UP000051216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root61 {ECO:0000313|EMBL:KRA25306.1,
RC   ECO:0000313|Proteomes:UP000051216};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KRA25306.1}.
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DR   EMBL; LMGU01000001; KRA25306.1; -; Genomic_DNA.
DR   RefSeq; WP_056223432.1; NZ_LMGU01000001.1.
DR   AlphaFoldDB; A0A0T2L0C5; -.
DR   STRING; 1736570.ASD65_13400; -.
DR   OrthoDB; 9803995at2; -.
DR   Proteomes; UP000051216; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000051216};
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         179
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         180
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT   BINDING         207
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         208..210
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT   BINDING         229..232
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ   SEQUENCE   286 AA;  30964 MW;  1AE1AD71BF1B573F CRC64;
     MPVVSLKEIV DRSFAERYGV PAINVFNDLT LEAVLAGAVQ ASSPVIVQTS VKTVRTMGAG
     LIAAMWRELT RDIPVPVALH LDHCPDRAVI TECLEHGWNS VLFDASELPV AENQRQTIEV
     VAEARRHGAH VEGEIESITG VEDDHGSDEE SVRQSLDVQL AFLRETGVDV FAPAIGNAHG
     SYKTTPVLDG ARITQIVDAH PVPIALHGGS GLSDDQFRDL IARGCAKVNI STALKERFMK
     SELAFLEGAR DRDSWDPPSL FRDTRAQVIE LVVGYAQVFG SAGKGH
//
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