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Database: UniProt
Entry: K1WDS1_MARBU
LinkDB: K1WDS1_MARBU
Original site: K1WDS1_MARBU 
ID   K1WDS1_MARBU            Unreviewed;       288 AA.
AC   K1WDS1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   22-FEB-2023, entry version 37.
DE   RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|RuleBase:RU366023};
DE            Short=FBP aldolase {ECO:0000256|RuleBase:RU366023};
DE            EC=4.1.2.13 {ECO:0000256|RuleBase:RU366023};
GN   ORFNames=MBM_06188 {ECO:0000313|EMBL:EKD15560.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD15560.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD15560.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD15560.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
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|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|RuleBase:RU366023}.
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. {ECO:0000256|RuleBase:RU366023}.
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DR   EMBL; JH921441; EKD15560.1; -; Genomic_DNA.
DR   RefSeq; XP_007294077.1; XM_007294015.1.
DR   AlphaFoldDB; K1WDS1; -.
DR   STRING; 1072389.K1WDS1; -.
DR   GeneID; 18762123; -.
DR   KEGG; mbe:MBM_06188; -.
DR   eggNOG; KOG4153; Eukaryota.
DR   HOGENOM; CLU_040088_4_0_1; -.
DR   InParanoid; K1WDS1; -.
DR   OMA; NNMEIVQ; -.
DR   OrthoDB; 1763470at2759; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
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   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; 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   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|RuleBase:RU366023};
KW   Lyase {ECO:0000256|RuleBase:RU366023};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3,
KW   ECO:0000256|RuleBase:RU366023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001359-3, ECO:0000256|RuleBase:RU366023}.
FT   ACT_SITE        86
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT   BINDING         87
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         110
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         186
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         217
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   288 AA;  31188 MW;  BFB1A5DD45E5871C CRC64;
     MSRPDLKDNR TMAILNAARD GGYAVPAVCC YNLESIIATV RAAEACRSPA IVQLFPWALE
     YAGSTLVLAA AEAAHSSSAP VTLHLDHAQT PELVRQAADI PAAFDGIMCD MSHYEKEENL
     ELTRELTEYC HRRGIISEAE PGRIEGGEDG VAATVDLEAV LTTPEQAEEF VSTGIELLAP
     AFGNVHGEYG PRGINLEYER LESVHKAVGD RVRLVLHGAD PFDETVFTKC IRAGVTKINI
     NKGVNKHYEK VQAEMRGKPL TTVIEAGTLA MQKAVENYMR ILGSAGKA
//
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