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ALFC_PINST
ID   ALFC_PINST              Reviewed;          71 AA.
AC   P84722;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Putative fructose-bisphosphate aldolase, chloroplastic;
DE            EC=4.1.2.13;
DE   AltName: Full=PS6;
DE   Flags: Fragments;
OS   Pinus strobus (Eastern white pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Strobus.
OX   NCBI_TaxID=3348;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Leaf {ECO:0000269|PubMed:16529377};
RX   PubMed=16529377; DOI=10.1094/mpmi-19-0150;
RA   Smith J.A., Blanchette R.A., Burnes T.A., Jacobs J.J., Higgins L.,
RA   Witthuhn B.A., David A.J., Gillman J.H.;
RT   "Proteomic comparison of needles from blister rust-resistant and
RT   susceptible Pinus strobus seedlings reveals upregulation of putative
RT   disease resistance proteins.";
RL   Mol. Plant Microbe Interact. 19:150-160(2006).
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:0000305};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 5.6,
CC       its MW is: 25.2 kDa. {ECO:0000269|PubMed:16529377}.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000255}.
CC   -!- CAUTION: The order of the peptides shown is unknown.
CC       {ECO:0000269|PubMed:16529377}.
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DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Glycolysis; Lyase; Plastid;
KW   Schiff base.
FT   CHAIN           <1..>71
FT                   /note="Putative fructose-bisphosphate aldolase,
FT                   chloroplastic"
FT                   /id="PRO_0000240610"
FT   NON_CONS        15..16
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        29..30
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        37..38
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        42..43
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        52..53
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        59..60
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        65..66
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_TER         71
FT                   /evidence="ECO:0000303|PubMed:16529377"
SQ   SEQUENCE   71 AA;  7141 MW;  77840B64DE586391 CRC64;
     TVVSIPNGPS ALAVKGILAM DESNATCGKG SYADELVTFE VACXGLDVAA SRYSEELVKA
     PSALTSVVTP G
 
 
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