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Database: UniProt
Entry: A0A1T4UUJ5_9GAMM
LinkDB: A0A1T4UUJ5_9GAMM
Original site: A0A1T4UUJ5_9GAMM 
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
//
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