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GLNA_VITSX
ID   GLNA_VITSX              Reviewed;          51 AA.
AC   P85087;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Glutamine synthetase;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
DE   Flags: Fragments;
OS   Vitis sp. (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis; unclassified Vitis.
OX   NCBI_TaxID=3604;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND INDUCTION.
RC   STRAIN=V.simpsonii cv. Pixiola X V.vinifera cv. Golden Muscat
RC   {ECO:0000269|PubMed:18931950}; TISSUE=Leaf {ECO:0000269|PubMed:18931950};
RX   PubMed=18931950; DOI=10.1007/s12010-008-8380-3;
RA   Vasanthaiah H.K.N., Katam R., Basha S.M.;
RT   "Characterization of unique and differentially expressed proteins in
RT   anthracnose-tolerant Florida hybrid bunch grapes.";
RL   Appl. Biochem. Biotechnol. 157:395-406(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC         phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC         Evidence={ECO:0000250|UniProtKB:Q56WN1};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000250|UniProtKB:Q56WN1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: By E.ampelina infection. {ECO:0000269|PubMed:18931950}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000255}.
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DR   AlphaFoldDB; P85087; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Direct protein sequencing; Ligase;
KW   Nitrogen fixation; Nucleotide-binding.
FT   CHAIN           1..>51
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000280228"
FT   NON_CONS        11..12
FT                   /evidence="ECO:0000303|PubMed:18931950"
FT   NON_CONS        21..22
FT                   /evidence="ECO:0000303|PubMed:18931950"
FT   NON_CONS        35..36
FT                   /evidence="ECO:0000303|PubMed:18931950"
FT   NON_TER         51
FT                   /evidence="ECO:0000303|PubMed:18931950"
SQ   SEQUENCE   51 AA;  5578 MW;  336DD02F7463405F CRC64;
     TLSGPVSDPA KNDGGFEVIK KHKEHIAAYG EGNERHETAD INTFLWGVAN R
 
 
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