ID M9WBJ8_9MOLU Unreviewed; 296 AA.
AC M9WBJ8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Fructose-bisphosphate aldolase class II {ECO:0000313|EMBL:AGJ90497.1};
GN Name=fbaA2 {ECO:0000313|EMBL:AGJ90497.1};
GN ORFNames=MPUT9231_0410 {ECO:0000313|EMBL:AGJ90497.1};
OS Mycoplasma putrefaciens Mput9231.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=1292033 {ECO:0000313|EMBL:AGJ90497.1, ECO:0000313|Proteomes:UP000012984};
RN [1] {ECO:0000313|EMBL:AGJ90497.1, ECO:0000313|Proteomes:UP000012984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mput9231 {ECO:0000313|EMBL:AGJ90497.1};
RX PubMed=23766410;
RA Dupuy V., Sirand-Pugnet P., Baranowski E., Barre A., Breton M., Couture C.,
RA Dordet-Frisoni E., Gaurivaud P., Jacob D., Lemaitre C., Manso-Silvan L.,
RA Nikolski M., Nouvel L.X., Poumarat F., Tardy F., Thebault P., Theil S.,
RA Citti C., Blanchard A., Thiaucourt F.;
RT "Complete Genome Sequence of Mycoplasma putrefaciens Strain 9231, One of
RT the Agents of Contagious Agalactia in Goats.";
RL Genome Announc. 1:e00354-13(2013).
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};
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DR EMBL; CP004357; AGJ90497.1; -; Genomic_DNA.
DR RefSeq; WP_015587166.1; NC_021083.1.
DR AlphaFoldDB; M9WBJ8; -.
DR KEGG; mput:MPUT9231_0410; -.
DR PATRIC; fig|1292033.3.peg.41; -.
DR eggNOG; COG0191; Bacteria.
DR HOGENOM; CLU_040088_0_1_14; -.
DR OrthoDB; 9803995at2; -.
DR Proteomes; UP000012984; Chromosome.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic 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 InterPro; IPR011289; Fruc_bis_ald_class-2.
DR NCBIfam; TIGR00167; cbbA; 1.
DR NCBIfam; TIGR01859; fruc_bis_ald; 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.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000012984};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 91
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 92
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 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 185
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 186
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 214
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 215..217
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 236..239
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ SEQUENCE 296 AA; 32435 MW; 3E71B9BBC00DD5E8 CRC64;
MPKLYHKRLV NATKMVNDAH KNKYAIGHFN INNLEWTKSI LEATQASNTP VILATSEGAI
KYMGGIETVV GMVNGLLDFL DITVPVALHL DHGQSVEMAK KCILAGYSSV MFDGSHLPYE
ENLKMTKELV EFAKEYEVSV EVEIGSIGGE EDGVVGQGEL GDPAQAKEIS TTGISMLAAG
IGNIHGKYPS WWTSLSFDTL NSLQKACNMP MVLHGGSGVP QEQVKKAISL GISKINVNTE
LQLAFRDATR KYIEEQKDLD DAKKGFDPRK LLKPGCDALK QTFLELTEWF GCKNKA
//
