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Database: UniProt
Entry: R5QP03_9PROT
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Original site: R5QP03_9PROT 
ID   R5QP03_9PROT            Unreviewed;       351 AA.
AC   R5QP03;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Fructose-1,6-bisphosphate aldolase {ECO:0000256|RuleBase:RU365019};
DE            Short=FBP aldolase {ECO:0000256|RuleBase:RU365019};
DE            EC=4.1.2.13 {ECO:0000256|RuleBase:RU365019};
GN   ORFNames=BN820_01503 {ECO:0000313|EMBL:CCZ22752.1};
OS   Acetobacter sp. CAG:977.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=1262685 {ECO:0000313|EMBL:CCZ22752.1, ECO:0000313|Proteomes:UP000018259};
RN   [1] {ECO:0000313|EMBL:CCZ22752.1, ECO:0000313|Proteomes:UP000018259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:977 {ECO:0000313|Proteomes:UP000018259};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-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|ARBA:ARBA00002181,
CC       ECO:0000256|RuleBase:RU365019}.
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:RU365019};
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};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU365019};
CC       Note=One is catalytic and the other provides a structural contribution.
CC       {ECO:0000256|RuleBase:RU365019};
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC       {ECO:0000256|ARBA:ARBA00005215}.
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:RU365019}.
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. {ECO:0000256|RuleBase:RU365019}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCZ22752.1}.
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DR   EMBL; CAZQ010000097; CCZ22752.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5QP03; -.
DR   STRING; 1262685.BN820_01503; -.
DR   UniPathway; UPA00109; UER00183.
DR   UniPathway; UPA00116; -.
DR   Proteomes; UP000018259; Unassembled WGS sequence.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
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; IPR006412; Fruct_bisP_Calv.
DR   NCBIfam; TIGR00167; cbbA; 1.
DR   NCBIfam; TIGR01521; FruBisAldo_II_B; 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; PS00602; ALDOLASE_CLASS_II_1; 1.
DR   PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE   3: Inferred from homology;
KW   Calvin cycle {ECO:0000256|ARBA:ARBA00022567};
KW   Glycolysis {ECO:0000256|RuleBase:RU365019};
KW   Lyase {ECO:0000256|RuleBase:RU365019};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3,
KW   ECO:0000256|RuleBase:RU365019};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018259};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001359-3, ECO:0000256|RuleBase:RU365019}.
FT   ACT_SITE        83
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT   BINDING         84
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         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         196
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         197
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT   BINDING         230
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         231..233
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT   BINDING         273..276
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ   SEQUENCE   351 AA;  38279 MW;  44E9BCA07614C1CF CRC64;
     MPMISLRQLL DHAAEYGYGM PAFNVNNMEQ ILAVMNAARK TNSPVIVQTS KGARSYAGDV
     MIHNMVQAAA EMYPELPICL HQDHGDSYKT CVTALANGWT SVMMDGSLKD GKPASHEYNA
     EVSAKVVETA HMIGASVEAE LGCIGSLETG KGEKEDGHGF EGALDKKQLL TDPDEAFDFV
     KQTNVDALAV AIGTSHGAYK FTRKPDGAIL SIDTIKKIHA KIPTVHLVMH GSSSVPQELQ
     DMINEFGGQI PQTYGVPIEE IQEGIKYGVR KVNVDTDCRM AMTGAIRKIF ATKPGEFDVR
     KYMGPAMEEM EKVCIARYEQ FGAAGHADKI KAIRLPEMAK RYASGELDHK I
//
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