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Database: UniProt
Entry: C9ABI8_ENTCA
LinkDB: C9ABI8_ENTCA
Original site: C9ABI8_ENTCA 
ID   C9ABI8_ENTCA            Unreviewed;       299 AA.
AC   C9ABI8;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013779};
GN   ORFNames=ECBG_02516 {ECO:0000313|EMBL:EEV40247.1};
OS   Enterococcus casseliflavus EC20.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=565655 {ECO:0000313|EMBL:EEV40247.1, ECO:0000313|Proteomes:UP000012675};
RN   [1] {ECO:0000313|EMBL:EEV40247.1, ECO:0000313|Proteomes:UP000012675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC20 {ECO:0000313|EMBL:EEV40247.1,
RC   ECO:0000313|Proteomes:UP000012675};
RG   The Broad Institute Genome Sequencing Platform;
RA   Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA   White J., Yandava C., Gilmore M., Manson J., Palmer K., Carniol K.,
RA   Lander E., Nusbaum C., Galagan J., Birren B.;
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEV40247.1, ECO:0000313|Proteomes:UP000012675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC20 {ECO:0000313|EMBL:EEV40247.1,
RC   ECO:0000313|Proteomes:UP000012675};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Russ C., Feldgarden M., Gilmore M., Manson J., Palmer K., Carniol K.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Enterococcus casseliflavus EC20 (899205).";
RL   Submitted (MAR-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};
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DR   EMBL; CP004856; EEV40247.1; -; Genomic_DNA.
DR   RefSeq; WP_015510352.1; NZ_AKCC01000001.1.
DR   AlphaFoldDB; C9ABI8; -.
DR   GeneID; 15143247; -.
DR   KEGG; ecas:ECBG_02516; -.
DR   eggNOG; COG0191; Bacteria.
DR   HOGENOM; CLU_040088_0_1_9; -.
DR   Proteomes; UP000012675; Chromosome.
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   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   Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012675};
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   299 AA;  32269 MW;  2494E61426A711D7 CRC64;
     MLVSGKEILS VAKEQGFAVP AFNAGSGQLL NAVMTACEEL QSPVMIAIHP DELSFLTDSF
     VSQVKYLANH SKVPVCIHLD HGASYEQVIH AIQLGFTSVM IDASHLPYDE NVAISKKVVE
     TAHVVGVSVE AELGTIGDTG NTVEGGVSEV IYTDPKVAQD FIEKTGVDSL AVAIGTAHGI
     YPKNIDPKLR LDILEEIEAL TDLPLVLHGG SSNPDEEIRK AVTMGINKIN ISSDIKIVFA
     SRLREILNSG NSEIREPNVL FPSCMEATKQ VAIEKIKLFK SDNKAQYYGL RGINESVTL
//
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