ID W9GLQ4_9MICO Unreviewed; 280 AA.
AC W9GLQ4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Fructose-bisphosphate aldolase {ECO:0000313|EMBL:EWT07000.1};
GN ORFNames=N864_13670 {ECO:0000313|EMBL:EWT07000.1};
OS Intrasporangium chromatireducens Q5-1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Intrasporangium.
OX NCBI_TaxID=584657 {ECO:0000313|EMBL:EWT07000.1, ECO:0000313|Proteomes:UP000019494};
RN [1] {ECO:0000313|Proteomes:UP000019494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q5-1 {ECO:0000313|Proteomes:UP000019494};
RA Liu H., Wang G.;
RT "Intrasporangium oryzae NRRL B-24470.";
RL Submitted (AUG-2013) 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:EWT07000.1}.
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DR EMBL; AWQS01000025; EWT07000.1; -; Genomic_DNA.
DR RefSeq; WP_034714280.1; NZ_AWQS01000025.1.
DR AlphaFoldDB; W9GLQ4; -.
DR PATRIC; fig|584657.3.peg.1054; -.
DR OrthoDB; 9803995at2; -.
DR Proteomes; UP000019494; 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 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:UP000019494};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 84
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 85
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 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 136
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 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"
SQ SEQUENCE 280 AA; 28936 MW; 67A44F9C5B9E35EE CRC64;
MPLATTSELV QQAREQGRGV PAFNVITLEH AEGIVRGAEQ AGVAVILQIS ENAVKFHGGR
LSPIAAASLA VARDAAVDVS VHLDHVEDVE LLHQAARDGL SSAMFDASVL DYADNVAATR
SAADWAHGAG IFLEAELGKV GGKDGAHAPG VRTDPDEARA FVGDTGVDAL AVAVGSSHAM
TDRTALLDVD LIHRLAAAVP VPLVLHGSSG VPDDQLRAAV RAGMVKINIG TILNVAFTSA
VRARLRADDR VVDPRRYLGV ARDEVAAVAG RLATVVGGAR
//