UniProt: A0A072ULB0

Database: UniProt
Entry: A0A072ULB0_MEDTR

LinkDB:  A0A072ULB0_MEDTR 
Original site:  A0A072ULB0_MEDTR

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (5)   
   InterPro (3)   
   Pfam (1)   
   PROSITE (1)   
Literature (2)   
   PubMed (2)   
All databases (14)   

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ID   A0A072ULB0_MEDTR        Unreviewed;       386 AA.
AC   A0A072ULB0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU003994};
DE            EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU003994};
GN   OrderedLocusNames=MTR_4g071880 {ECO:0000313|EMBL:KEH30472.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:KEH30472.1, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:KEH30472.1, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:KEH30472.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:KEH30472,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA   Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA   Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA   Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA   Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA   Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA   Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA   Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA   Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA   Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA   Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA   Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA   Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA   Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA   Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA   Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA   Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA   Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA   Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA   Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA   Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [2] {ECO:0000313|EMBL:KEH30472.1, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=A17 {ECO:0000313|EMBL:KEH30472.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:KEH30472,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [3] {ECO:0000313|EnsemblPlants:KEH30472}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH30472};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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:RU003994};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC       {ECO:0000256|ARBA:ARBA00004714}.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000256|ARBA:ARBA00010387, ECO:0000256|RuleBase:RU003994}.
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DR   EMBL; CM001220; KEH30472.1; -; Genomic_DNA.
DR   RefSeq; XP_013456441.1; XM_013600987.1.
DR   AlphaFoldDB; A0A072ULB0; -.
DR   STRING; 3880.A0A072ULB0; -.
DR   PaxDb; 3880-AES89264; -.
DR   EnsemblPlants; KEH30472; KEH30472; MTR_4g071880.
DR   Gramene; KEH30472; KEH30472; MTR_4g071880.
DR   eggNOG; KOG1557; Eukaryota.
DR   HOGENOM; CLU_031243_0_1_1; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000002051; Chromosome 4.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IBA:GO_Central.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   CDD; cd00948; FBP_aldolase_I_a; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR029768; Aldolase_I_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000741; FBA_I.
DR   NCBIfam; NF033379; FrucBisAld_I; 1.
DR   PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR11627:SF16; FRUCTOSE-BISPHOSPHATE ALDOLASE, CHLOROPLASTIC; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|RuleBase:RU003994};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003994};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270}.
SQ   SEQUENCE   386 AA;  41965 MW;  AE18108353AB71EF CRC64;
     MASASASLFK SSIVLDKSEW VKGQTLRQSS VAAVRCNPAA PSSLTIRAGS YANELVKTAK
     TIASPGRGIL AMDESNATCG KSLASIGLEN TEVNRPAWRT LLVTVPSLGE YISGAILFEE
     TLYQSTTDGR KIVDVLIEVW CPLLVPMMRW CQGLDGLASR SAAYYQQDAH FAKWRTVLSI
     PNGPSALAVK EAAWGLARYA AISQDNGLVP IVEPEILLDG EHSIDRTFEV AQKVWAEVFF
     YLAENNVQFE GILLKPSMVT PGAESKDKVS SATVADYILK LLHRRIPPAV PGIMFLSGGQ
     SEVEATLNLN AMNQSPNPWH VSFSYARALQ NTALKTWGGR IENVQAAQEA LLFRAKSNSL
     AQLGKYTGEG ESEEAKKELF VKGYSY
//

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