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[1]
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NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Gerbel;
TISSUE=Leaf;
DOI=10.1007/BF00042228; PubMed=8790288 [NCBI, ExPASy, EBI, Israel, Japan]
Baier M.,
Dietz K.-J.;
"Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases.";
Plant Mol. Biol. 31:553-564(1996).
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- FUNCTION: May be an antioxidant enzyme particularly important in the developing shoot and photosynthesizing leaf.
- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
- SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By similarity).
- SUBCELLULAR LOCATION: Plastid, chloroplast (By similarity).
- TISSUE SPECIFICITY: Expressed in leaf blade, sheath, basiplast, stem and green spike. Maximal expression in young developing shoots segments where cell division and elongation take place. Not expressed in roots.
- DEVELOPMENTAL STAGE: Maximal levels are seen in 4-day old seedlings and decline during aging of the seedling.
- PTM: The Cys-64-SH group is the primary site of oxidation by H(2)O(2), and the oxidized Cys-64 (probably Cys-SOH) rapidly reacts with Cys-185-SH of the other subunit to form an intermolecular disulfide. This disulfide might subsequently be reduced by thioredoxin (By similarity).
- SIMILARITY: Belongs to the ahpC/TSA family.
- SIMILARITY: Contains 1 thioredoxin domain.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 210 AA [This is the length of the partial sequence of the unprocessed precursor] |
Molecular weight: 23299 Da [This is the MW of the partial sequence of the unprocessed precursor] |
CRC64: 4DD488179D6BCAC9 [This is a checksum on the sequence] |
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10 20 30 40 50 60
DARARSFVAR AAAEYDLPLV GNKAPDFAAE AVFDQEFINV KLSDYIGKKY VILFFYPLDF
70 80 90 100 110 120
TFVCPTEITA FSDRHEEFEK INTEILGVSV DSVFSHLAWV QTERKSGGLG DLKYPLVSDV
130 140 150 160 170 180
TKSISKSFGV LIPDQGIALR GLFIIDKEGV IQHSTINNLG IGRSVDETLR TLQALQYVKK
190 200 210
PDEVCPAGWK PGEKSMKPDP KGSKEYFAAI
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Q96468 in FASTA format |
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