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Protein

Ferredoxin-dependent glutamate synthase 1, chloroplastic/mitochondrial

Gene

GLU1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in glutamate biosynthesis in leaf. Required for the reassimilation of ammonium ions generated during photorespiration.4 Publications

Catalytic activityi

2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+.

Cofactori

Protein has several cofactor binding sites:

Pathwayi: L-glutamate biosynthesis via GLT pathway

This protein is involved in step 1 of the subpathway that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine (ferredoxin route).
Proteins known to be involved in this subpathway in this organism are:
  1. Ferredoxin-dependent glutamate synthase 2, chloroplastic (GLU2), Ferredoxin-dependent glutamate synthase 1, chloroplastic/mitochondrial (GLU1)
This subpathway is part of the pathway L-glutamate biosynthesis via GLT pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine (ferredoxin route), the pathway L-glutamate biosynthesis via GLT pathway and in Amino-acid biosynthesis.

Pathwayi: nitrogen metabolism

This protein is involved in the pathway nitrogen metabolism, which is part of Energy metabolism.
View all proteins of this organism that are known to be involved in the pathway nitrogen metabolism and in Energy metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei106 – 1061For GATase activityBy similarity
Metal bindingi1237 – 12371Iron-sulfur (3Fe-4S)By similarity
Metal bindingi1243 – 12431Iron-sulfur (3Fe-4S)By similarity
Metal bindingi1248 – 12481Iron-sulfur (3Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1184 – 124158FMNBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • ammonia assimilation cycle Source: GO_Central
  • glutamate biosynthetic process Source: GO_Central
  • L-glutamate biosynthetic process Source: UniProtKB-UniPathway
  • photorespiration Source: TAIR
  • positive regulation of glycine hydroxymethyltransferase activity Source: TAIR
  • response to light stimulus Source: UniProtKB
  • response to sucrose Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Glutamate biosynthesis

Keywords - Ligandi

3Fe-4S, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT5G04140-MONOMER.
ARA:GQT-2064-MONOMER.
BRENDAi1.4.7.1. 399.
UniPathwayiUPA00045.
UPA00634; UER00691.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferredoxin-dependent glutamate synthase 1, chloroplastic/mitochondrial (EC:1.4.7.1)
Alternative name(s):
Fd-GOGAT 1
Gene namesi
Name:GLU1
Synonyms:GLS1
Ordered Locus Names:At5g04140
ORF Names:F21E1_60
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G04140.

Subcellular locationi

  • Plastidchloroplast stroma
  • Mitochondrion matrix

  • Note: Dual targeting is supposed to depend on alternative initiation: MET-1 or MET-3 for chloroplast or mitochondrion location, respectively.1 Publication

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast stroma Source: TAIR
  • membrane Source: TAIR
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Mitochondrion, Plastid

Pathology & Biotechi

Disruption phenotypei

Displays photorespiratory chlorosis when grown at ambient CO2.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1270 – 12701L → F in glu1-201; Abolishes interaction with SHM1. Displays photorespiratory chlorosis when grown at ambient CO2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 105105Chloroplast and mitochondrionSequence analysisAdd
BLAST
Chaini106 – 16221517Ferredoxin-dependent glutamate synthase 1, chloroplastic/mitochondrialPRO_0000011614Add
BLAST

Proteomic databases

PaxDbiQ9ZNZ7.
PRIDEiQ9ZNZ7.

PTM databases

iPTMnetiQ9ZNZ7.

Expressioni

Tissue specificityi

Highly expressed in leaves. High expression in the leaf mesophyll and phloem companion cell-sieve element complex.2 Publications

Inductioni

Up-regulated by GATA21/GNC and GATA22/CGA1. Induced by light or sucrose.2 Publications

Gene expression databases

ExpressionAtlasiQ9ZNZ7. baseline and differential.
GenevisibleiQ9ZNZ7. AT.

Interactioni

Subunit structurei

Interacts with SHM1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SHM1Q9SZJ52EBI-2292564,EBI-2292536

Protein-protein interaction databases

BioGridi15572. 3 interactions.
IntActiQ9ZNZ7. 2 interactions.
STRINGi3702.AT5G04140.2.

Structurei

3D structure databases

ProteinModelPortaliQ9ZNZ7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini106 – 505400Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glutamate synthase family.Curated
Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase, Transit peptide

Phylogenomic databases

eggNOGiKOG0399. Eukaryota.
COG0067. LUCA.
COG0069. LUCA.
COG0070. LUCA.
HOGENOMiHOG000031558.
InParanoidiQ9ZNZ7.
KOiK00284.
OMAiTILDINY.

Family and domain databases

Gene3Di2.160.20.60. 1 hit.
3.20.20.70. 2 hits.
3.60.20.10. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR017932. GATase_2_dom.
IPR002489. Glu_synth_asu_C.
IPR006982. Glu_synth_centr_N.
IPR002932. Glu_synthdom.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PfamiPF00310. GATase_2. 1 hit.
PF04898. Glu_syn_central. 1 hit.
PF01645. Glu_synthase. 1 hit.
PF01493. GXGXG. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
SSF69336. SSF69336. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9ZNZ7-1) [UniParc]FASTAAdd to basket

Also known as: Short

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAMQSLSPVP KLLSTTPSSV LSSDKNFFFV DFVGLYCKSK RTRRRLRGDS
60 70 80 90 100
SSSSRSSSSL SRLSSVRAVI DLERVHGVSE KDLSSPSALR PQVANLEDIL
110 120 130 140 150
SERGACGVGF IANLDNIPSH GVVKDALIAL GCMEHRGGCG ADNDSGDGSG
160 170 180 190 200
LMSSIPWDFF NVWAKEQSLA PFDKLHTGVG MIFLPQDDTF MQEAKQVIEN
210 220 230 240 250
IFEKEGLQVL GWREVPVNVP IVGKNARETM PNIQQVFVKI AKEDSTDDIE
260 270 280 290 300
RELYICRKLI ERAVATESWG TELYFCSLSN QTIVYKGMLR SEALGLFYLD
310 320 330 340 350
LQNELYESPF AIYHRRYSTN TSPRWPLAQP MRFLGHNGEI NTIQGNLNWM
360 370 380 390 400
QSREASLKAA VWNGRENEIR PFGNPRGSDS ANLDSAAEIM IRSGRTPEEA
410 420 430 440 450
LMILVPEAYK NHPTLSVKYP EVVDFYDYYK GQMEAWDGPA LLLFSDGKTV
460 470 480 490 500
GACLDRNGLR PARYWRTSDN FVYVASEVGV VPVDEAKVTM KGRLGPGMMI
510 520 530 540 550
AVDLVNGQVY ENTEVKKRIS SFNPYGKWIK ENSRFLKPVN FKSSTVMENE
560 570 580 590 600
EILRSQQAFG YSSEDVQMVI ESMASQGKEP TFCMGDDIPL AGLSQRPHML
610 620 630 640 650
YDYFKQRFAQ VTNPAIDPLR EGLVMSLEVN IGKRGNILEL GPENASQVIL
660 670 680 690 700
SNPVLNEGAL EELMKDQYLK PKVLSTYFDI RKGVEGSLQK ALYYLCEAAD
710 720 730 740 750
DAVRSGSQLL VLSDRSDRLE PTRPSIPIML AVGAVHQHLI QNGLRMSASI
760 770 780 790 800
VADTAQCFST HHFACLVGYG ASAVCPYLAL ETCRQWRLSN KTVAFMRNGK
810 820 830 840 850
IPTVTIEQAQ KNYTKAVNAG LLKILSKMGI SLLSSYCGAQ IFEIYGLGQD
860 870 880 890 900
VVDLAFTGSV SKISGLTFDE LARETLSFWV KAFSEDTTKR LENFGFIQFR
910 920 930 940 950
PGGEYHSNNP EMSKLLHKAV REKSETAYAV YQQHLSNRPV NVLRDLLEFK
960 970 980 990 1000
SDRAPIPVGK VEPAVAIVQR FCTGGMSLGA ISRETHEAIA IAMNRIGGKS
1010 1020 1030 1040 1050
NSGEGGEDPI RWKPLTDVVD GYSPTLPHLK GLQNGDIATS AIKQVASGRF
1060 1070 1080 1090 1100
GVTPTFLVNA DQLEIKVAQG AKPGEGGQLP GKKVSAYIAR LRSSKPGVPL
1110 1120 1130 1140 1150
ISPPPHHDIY SIEDLAQLIF DLHQINPNAK VSVKLVAEAG IGTVASGVAK
1160 1170 1180 1190 1200
GNADIIQISG HDGGTGASPI SSIKHAGGPW ELGLTETHQT LIANGLRERV
1210 1220 1230 1240 1250
ILRVDGGLKS GVDVLMAAAM GADEYGFGSL AMIATGCVMA RICHTNNCPV
1260 1270 1280 1290 1300
GVASQREELR ARFPGVPGDL VNYFLYVAEE VRGILAQLGY NSLDDIIGRT
1310 1320 1330 1340 1350
ELLRPRDISL VKTQHLDLSY LLSSVGTPSL SSTEIRKQEV HTNGPVLDDD
1360 1370 1380 1390 1400
ILADPLVIDA IENEKVVEKT VKICNVDRAA CGRVAGVIAK KYGDTGFAGQ
1410 1420 1430 1440 1450
VNLTFLGSAG QSFGCFLIPG MNIRLIGESN DYVGKGMAGG EIVVTPVEKI
1460 1470 1480 1490 1500
GFVPEEATIV GNTCLYGATG GQIFARGKAG ERFAVRNSLA EAVVEGTGDH
1510 1520 1530 1540 1550
CCEYMTGGCV VVLGKVGRNV AAGMTGGLAY LLDEDDTLLP KINREIVKIQ
1560 1570 1580 1590 1600
RVTAPAGELQ LKSLIEAHVE KTGSSKGATI LNEWEKYLPL FWQLVPPSEE
1610 1620
DTPEASAAYV RTSTGEVTFQ SA
Length:1,622
Mass (Da):176,752
Last modified:May 29, 2013 - v3
Checksum:iFAE7D097490F8A97
GO
Isoform 2 (identifier: Q9ZNZ7-2) [UniParc]FASTAAdd to basket

Also known as: Long

The sequence of this isoform differs from the canonical sequence as follows:
     92-92: Q → QVRFFTDINFTNTQRAKFHPLWGSFKQ

Note: May be due to an intron retention. No experimental confirmation available.
Show »
Length:1,648
Mass (Da):179,920
Checksum:i58790CE711DCBF6A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961L → W in AAC78551 (PubMed:9596633).Curated
Sequence conflicti211 – 2111G → R in AAC78551 (PubMed:9596633).Curated
Sequence conflicti385 – 3851S → C in CAA70862 (PubMed:9057836).Curated
Sequence conflicti621 – 6244EGLV → KVWF in CAA70862 (PubMed:9057836).Curated
Sequence conflicti734 – 7341A → T in CAA70862 (PubMed:9057836).Curated
Sequence conflicti1473 – 14742IF → DI in CAA70862 (PubMed:9057836).Curated
Sequence conflicti1585 – 15851E → K in AAC78551 (PubMed:9596633).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei92 – 921Q → QVRFFTDINFTNTQRAKFHP LWGSFKQ in isoform 2. 1 PublicationVSP_046513

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09667 mRNA. Translation: CAA70862.1.
U39287 mRNA. Translation: AAC78551.1.
AL391716 Genomic DNA. Translation: CAC05496.1.
CP002688 Genomic DNA. Translation: AED90703.1.
CP002688 Genomic DNA. Translation: AED90704.1.
RefSeqiNP_568134.1. NM_120496.2. [Q9ZNZ7-1]
NP_850763.1. NM_180432.2. [Q9ZNZ7-2]
UniGeneiAt.21961.
At.67926.

Genome annotation databases

EnsemblPlantsiAT5G04140.1; AT5G04140.1; AT5G04140. [Q9ZNZ7-1]
GeneIDi830292.
KEGGiath:AT5G04140.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09667 mRNA. Translation: CAA70862.1.
U39287 mRNA. Translation: AAC78551.1.
AL391716 Genomic DNA. Translation: CAC05496.1.
CP002688 Genomic DNA. Translation: AED90703.1.
CP002688 Genomic DNA. Translation: AED90704.1.
RefSeqiNP_568134.1. NM_120496.2. [Q9ZNZ7-1]
NP_850763.1. NM_180432.2. [Q9ZNZ7-2]
UniGeneiAt.21961.
At.67926.

3D structure databases

ProteinModelPortaliQ9ZNZ7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi15572. 3 interactions.
IntActiQ9ZNZ7. 2 interactions.
STRINGi3702.AT5G04140.2.

PTM databases

iPTMnetiQ9ZNZ7.

Proteomic databases

PaxDbiQ9ZNZ7.
PRIDEiQ9ZNZ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G04140.1; AT5G04140.1; AT5G04140. [Q9ZNZ7-1]
GeneIDi830292.
KEGGiath:AT5G04140.

Organism-specific databases

TAIRiAT5G04140.

Phylogenomic databases

eggNOGiKOG0399. Eukaryota.
COG0067. LUCA.
COG0069. LUCA.
COG0070. LUCA.
HOGENOMiHOG000031558.
InParanoidiQ9ZNZ7.
KOiK00284.
OMAiTILDINY.

Enzyme and pathway databases

UniPathwayiUPA00045.
UPA00634; UER00691.
BioCyciARA:AT5G04140-MONOMER.
ARA:GQT-2064-MONOMER.
BRENDAi1.4.7.1. 399.

Miscellaneous databases

PROiQ9ZNZ7.

Gene expression databases

ExpressionAtlasiQ9ZNZ7. baseline and differential.
GenevisibleiQ9ZNZ7. AT.

Family and domain databases

Gene3Di2.160.20.60. 1 hit.
3.20.20.70. 2 hits.
3.60.20.10. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR017932. GATase_2_dom.
IPR002489. Glu_synth_asu_C.
IPR006982. Glu_synth_centr_N.
IPR002932. Glu_synthdom.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PfamiPF00310. GATase_2. 1 hit.
PF04898. Glu_syn_central. 1 hit.
PF01645. Glu_synthase. 1 hit.
PF01493. GXGXG. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
SSF69336. SSF69336. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and regulation of ferredoxin-dependent glutamase synthase from Arabidopsis thaliana. Cloning of cDNA expression in different tissues of wild-type and gltS mutant strains, and light induction."
    Suzuki A., Rothstein S.
    Eur. J. Biochem. 243:708-718(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: cv. Columbia.
  2. "Arabidopsis gls mutants and distinct Fd-GOGAT genes. Implications for photorespiration and primary nitrogen assimilation."
    Coschigano K.T., Melo-Oliveira R., Lim J., Coruzzi G.M.
    Plant Cell 10:741-752(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INDUCTION BY LIGHT AND SUGAR.
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Assimilation of excess ammonium into amino acids and nitrogen translocation in Arabidopsis thaliana--roles of glutamate synthases and carbamoylphosphate synthetase in leaves."
    Potel F., Valadier M.H., Ferrario-Mery S., Grandjean O., Morin H., Gaufichon L., Boutet-Mercey S., Lothier J., Rothstein S.J., Hirose N., Suzuki A.
    FEBS J. 276:4061-4076(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
  6. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  7. "Arabidopsis photorespiratory serine hydroxymethyltransferase activity requires the mitochondrial accumulation of ferredoxin-dependent glutamate synthase."
    Jamai A., Salome P.A., Schilling S.H., Weber A.P., McClung C.R.
    Plant Cell 21:595-606(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHM1, SUBCELLULAR LOCATION, DUAL TARGETING, FUNCTION, MUTAGENESIS OF LEU-1270, DISRUPTION PHENOTYPE.
  8. "Analysis of glutamate homeostasis by overexpression of Fd-GOGAT gene in Arabidopsis thaliana."
    Ishizaki T., Ohsumi C., Totsuka K., Igarashi D.
    Amino Acids 38:943-950(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "GNC and CGA1 modulate chlorophyll biosynthesis and glutamate synthase (GLU1/Fd-GOGAT) expression in Arabidopsis."
    Hudson D., Guevara D., Yaish M.W., Hannam C., Long N., Clarke J.D., Bi Y.M., Rothstein S.J.
    PLoS ONE 6:E26765-E26765(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY GATA21/GNC AND GATA22/CGA1.

Entry informationi

Entry nameiGLTB1_ARATH
AccessioniPrimary (citable) accession number: Q9ZNZ7
Secondary accession number(s): P93649
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 29, 2013
Last modified: May 11, 2016
This is version 154 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.