ID A0A0F0KRS2_9MICO Unreviewed; 287 AA.
AC A0A0F0KRS2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Fructose-bisphosphate aldolase {ECO:0000313|EMBL:KJL23617.1};
DE EC=4.1.2.13 {ECO:0000313|EMBL:KJL23617.1};
GN Name=fba_1 {ECO:0000313|EMBL:KJL23617.1};
GN ORFNames=RN50_00955 {ECO:0000313|EMBL:KJL23617.1};
OS Microbacterium foliorum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=104336 {ECO:0000313|EMBL:KJL23617.1, ECO:0000313|Proteomes:UP000033572};
RN [1] {ECO:0000313|EMBL:KJL23617.1, ECO:0000313|Proteomes:UP000033572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12966 {ECO:0000313|EMBL:KJL23617.1,
RC ECO:0000313|Proteomes:UP000033572};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL23617.1}.
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DR EMBL; JYIU01000035; KJL23617.1; -; Genomic_DNA.
DR RefSeq; WP_045253373.1; NZ_JYIU01000035.1.
DR AlphaFoldDB; A0A0F0KRS2; -.
DR KEGG; mfol:DXT68_04490; -.
DR PATRIC; fig|104336.4.peg.979; -.
DR Proteomes; UP000033572; 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:KJL23617.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000033572};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 80
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 81
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 102
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 178
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
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 287 AA; 30965 MW; 18760A6731F0EE66 CRC64;
MLYTGKSILD VANEHNFAIP AFNISDWAMF TGIIDISEEL DAPVIIAIHP DEVSHVTTDL
IAAMHSRAHR ASVPVAIHWD HGGTYEQMIT AIKSGFTSVM IDASLLPFEE NVALTRKVVE
AAHAVGIQVE GELGTIGAND SYGESGAAEI IYTNPDDAVR FVQETGVDSL AIAIGTSHGL
YPSDKNPELR HDLLEQIKAA VGIPLVLHGG SSNPDAELKR AVELGVNKIN ISSDIKVSYH
NRMREILGTD ERLREPNAIQ PEPIAAMKAT AAEKIRLFGA DGKAELY
//
