ID A0A1T4UUJ5_9GAMM Unreviewed; 284 AA.
AC A0A1T4UUJ5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Fructose-bisphosphate aldolase, class II {ECO:0000313|EMBL:SKA56334.1};
GN ORFNames=SAMN02745132_02552 {ECO:0000313|EMBL:SKA56334.1};
OS Enterovibrio nigricans DSM 22720.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Enterovibrio.
OX NCBI_TaxID=1121868 {ECO:0000313|EMBL:SKA56334.1, ECO:0000313|Proteomes:UP000190162};
RN [1] {ECO:0000313|Proteomes:UP000190162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22720 {ECO:0000313|Proteomes:UP000190162};
RA Varghese N., Submissions S.;
RL Submitted (FEB-2017) 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};
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DR EMBL; FUXU01000031; SKA56334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4UUJ5; -.
DR OrthoDB; 9803995at2; -.
DR Proteomes; UP000190162; 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; 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 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 176
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 204
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 284 AA; 30776 MW; C08CAC5CB8C19FC3 CRC64;
MLVTLNDILP LEAQSSSAVA CCNVFGIEEA KAIISAAEHL NRPVILAVNK DMVDLAGVEA
MAGLLLPLAE SSDTQVCVHL DHCYEEAIVY RAIHAGFTSV MFDGSQLPLE ENIRRTRQVV
NVAHAVGVSV EGELGSVPYQ EGRDHIKSEF TASAEATIYA NESGIDALAV SVGNVHRMTE
AGSPIDFALL EEIEAVTTLP LVIHGTTGIT EADLLRLKTQ RIAKFNVGTT LRMAFGNAIR
EAMEIEPDKF DKQYFAGKAI PALQQEAIRV LSLLSSPRPI RERR
//