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Database: UniProt
Entry: H6RRH8_BLASD
LinkDB: H6RRH8_BLASD
Original site: H6RRH8_BLASD 
ID   H6RRH8_BLASD            Unreviewed;       344 AA.
AC   H6RRH8;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013779, ECO:0000256|RuleBase:RU366023};
DE            Short=FBP aldolase {ECO:0000256|RuleBase:RU366023};
DE            EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU366023};
GN   Name=fba {ECO:0000313|EMBL:CCG05460.1};
GN   OrderedLocusNames=BLASA_4663 {ECO:0000313|EMBL:CCG05460.1};
OS   Blastococcus saxobsidens (strain DD2).
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG05460.1, ECO:0000313|Proteomes:UP000007517};
RN   [1] {ECO:0000313|EMBL:CCG05460.1, ECO:0000313|Proteomes:UP000007517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD2 {ECO:0000313|EMBL:CCG05460.1,
RC   ECO:0000313|Proteomes:UP000007517};
RX   PubMed=22535935; DOI=10.1128/JB.00320-12;
RA   Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA   Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA   Gury J., Pujic P., Normand P.;
RT   "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT   Bacterium.";
RL   J. Bacteriol. 194:2752-2753(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA   Genoscope.;
RT   "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone
CC       phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate
CC       (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and
CC       the reverse reaction in glycolysis. {ECO:0000256|RuleBase:RU366023}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC         phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC         ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00000441,
CC         ECO:0000256|RuleBase:RU366023};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001359-3,
CC         ECO:0000256|RuleBase:RU366023};
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       ECO:0000256|RuleBase:RU366023};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC       {ECO:0000256|ARBA:ARBA00004714, ECO:0000256|RuleBase:RU366023}.
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. {ECO:0000256|ARBA:ARBA00005812, ECO:0000256|RuleBase:RU366023}.
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DR   EMBL; FO117623; CCG05460.1; -; Genomic_DNA.
DR   RefSeq; WP_014378327.1; NC_016943.1.
DR   AlphaFoldDB; H6RRH8; -.
DR   STRING; 1146883.BLASA_4663; -.
DR   KEGG; bsd:BLASA_4663; -.
DR   eggNOG; COG0191; Bacteria.
DR   HOGENOM; CLU_036923_1_0_11; -.
DR   OMA; PRTWGKL; -.
DR   OrthoDB; 9803995at2; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000007517; Chromosome.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000771; FBA_II.
DR   InterPro; IPR006411; Fruct_bisP_bact.
DR   NCBIfam; TIGR00167; cbbA; 1.
DR   NCBIfam; TIGR01520; FruBisAldo_II_A; 1.
DR   PANTHER; PTHR30559:SF0; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR30559; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 2; 1.
DR   Pfam; PF01116; F_bP_aldolase; 1.
DR   PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR   PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU366023};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU366023};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001359-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007517};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001359-3}.
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT   BINDING         96
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         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         212
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         213
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT   BINDING         252
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         253..255
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT   BINDING         274..277
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ   SEQUENCE   344 AA;  36774 MW;  FF136912116E6BC0 CRC64;
     MPIATPEVYA DMINRAKEGG FAYPAINCTS SETVNAALRG FADAGSDGII QFSTGGAEFG
     SGTRVKDMVT GAVALAEFTH VVAEKYPVNV ALHTDHCPKD KLDSYVRPLI ALSKDRVDAG
     QEPLFQSHMW DGSAIELTEN LDIAEELMER AAAAKIVLEL EIGIVGGEED GVVAEINEKL
     YTADGDFLRT AQQLGLGERG VYLLAATFGN VHGVYKPGNV KLRPDVLQRG QALVAKEFDL
     GEGAKPFNLV FHGGSGSAES EIREALSYGV VKMNVDTDTQ YAFTRPIAGH MLSNYDGVLK
     IDGEVGNKKA YDPRSYLKAA ETNMAARVVE ACEHLLSAGQ SQGA
//
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