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Protein

Ferredoxin-dependent glutamate synthase 2, chloroplastic

Gene

GLU2

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

Functioni

May play a role in primary nitrogen assimilation in roots. Could supply a constitutive level of glutamate to maintain a basal level of protein synthesis.2 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 sitei108 – 1081For GATase activityBy similarity
Metal bindingi1239 – 12391Iron-sulfur (3Fe-4S)By similarity
Metal bindingi1245 – 12451Iron-sulfur (3Fe-4S)By similarity
Metal bindingi1250 – 12501Iron-sulfur (3Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1186 – 124358FMNBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

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:AT2G41220-MONOMER.
BRENDAi1.4.7.1. 399.
UniPathwayiUPA00045.
UPA00634; UER00691.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferredoxin-dependent glutamate synthase 2, chloroplastic (EC:1.4.7.1)
Alternative name(s):
Fd-GOGAT 2
Gene namesi
Name:GLU2
Ordered Locus Names:At2g41220
ORF Names:F13H10.23
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G41220.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast stroma Source: UniProtKB-SubCell
  • plastid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. The glutamate and glutamine levels were unaffected.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 107107ChloroplastBy similarityAdd
BLAST
Chaini108 – 16291522Ferredoxin-dependent glutamate synthase 2, chloroplasticPRO_0000011615Add
BLAST

Proteomic databases

PaxDbiQ9T0P4.
PRIDEiQ9T0P4.

PTM databases

iPTMnetiQ9T0P4.

Expressioni

Tissue specificityi

Expressed predominantly in roots and slightly in leaves. Low expression in the leaf mesophyll and phloem companion cell-sieve element complex.2 Publications

Gene expression databases

GenevisibleiQ9T0P4. AT.

Interactioni

Protein-protein interaction databases

BioGridi4058. 1 interaction.
STRINGi3702.AT2G41220.1.

Structurei

3D structure databases

ProteinModelPortaliQ9T0P4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini108 – 507400Glutamine 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.
InParanoidiQ9T0P4.
KOiK00284.
OMAiHGRENDI.
PhylomeDBiQ9T0P4.

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]

Sequencei

Sequence statusi: Complete.

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

Q9T0P4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALQSPGATG ASSSVSRLLS SAKLSSTKTI FSVDFVRSYC ISKGTKRRNE
60 70 80 90 100
LSGFRGYSPL LKSSLRSPFS VKAILNSDRA AGDASSSFSD LKPQVAYLED
110 120 130 140 150
IISERGACGV GFIANLENKA THKIVNDALI ALGCMEHRGG CGSDNTSGDG
160 170 180 190 200
SGLMTSIPWD LFNEWAEKQG IASFDRTHTG VGMLFLPRDD NIRKEAKKVI
210 220 230 240 250
TSIFEKEGLE VLGWRDVPVE ASIVGHNAKQ TMPNTEQVFV RIVKDDKVDD
260 270 280 290 300
VERELYICRK LIERAVASES WASELYFSSL SNQTIVYKGM LRSEVLGLFY
310 320 330 340 350
PDLQNDLYKS PFAIYHRRFS TNTSPRWHLA QPMRFLGHNG EINTIQGNLN
360 370 380 390 400
WMTSREASLR SPVWHGREND IRPISNPKAS DSANLDSAAE LLIRSGRTPE
410 420 430 440 450
ESLMILVPEA YKNHPTLMIK YPEAVDFYDY YKGQMEPWDG PALVLFSDGK
460 470 480 490 500
TVGACLDRNG LRPARYWRTS DNVVYVASEV GVLPMDESKV TMKGRLGPGM
510 520 530 540 550
MISVDLENGQ VYENTEVKKR VASYNPYGKW VSENLRNLKP SNYLSSAILE
560 570 580 590 600
TDETLRRQQA FGYSSEDVQM VIESMAAQGK EPTFCMGDDT PVAVLSQKPH
610 620 630 640 650
MLYDYFKQRF AQVTNPAIDP LREGLVMSLE VNIGKRGNIL EVGPQNVSQV
660 670 680 690 700
VLSGPVLNER ELEGLLGDPL LKSQILPTFF DIRRGIEGSL KKGLLKLCEA
710 720 730 740 750
ADEAVRNGSQ VLVLSDRSDN PEPTRPAIPM LLAVGAVHQH LIQNGLRMSA
760 770 780 790 800
SIIADTAQCF STHHFACLIG YGASAICPHL ALETCRQWRL SNKTVNMMRN
810 820 830 840 850
GKMPTVTMEQ AQKNYRKAVN TGLLKVLSKM GISLFSSYCG AQIFEIYGLG
860 870 880 890 900
NEVVEFSFRG SASQIGGLTL DELARETLTF WVRAFSEDTA KRLENFGFIQ
910 920 930 940 950
FRPGGEYHGN NPEMSKLLHK AVREKSETAY AVYQQHLANR PITVFRDLLE
960 970 980 990 1000
FKSDRNPIPV GKVEPASSIV ERFCTGGMSL GAISRETHET IAIAMNRLGG
1010 1020 1030 1040 1050
KSNSGEGGED PIRWKPLTDV VDGYSSTLPH LKGLRNGDTA TSAIKQVASG
1060 1070 1080 1090 1100
RFGVTPTFLV NADQLEIKVA QGAKPGEGGQ LPGKKVSAYI ARLRNSKPGV
1110 1120 1130 1140 1150
PLISPPPHHD IYSIEDLAQL IFDLHQVNPK AKVSVKLVSE TGIGTVASGV
1160 1170 1180 1190 1200
AKANADIIQI SGYDGGTGAS PISSIKHAGG PWELGLAETQ KTLIGNGLRE
1210 1220 1230 1240 1250
RVIIRVDGGF KSGVDVLIAA AMGADEYGFG TLAMIATGCI MARICHTNNC
1260 1270 1280 1290 1300
PVGVASQREE LRARFPGLPG DLVNFFLYIA EEVRGILAQL GYEKLDDIIG
1310 1320 1330 1340 1350
RTDLLKARDI SLVKTHLDLS YLLSSVGLPK RSSTSIRKQE VHSNGPVLDD
1360 1370 1380 1390 1400
TLLQDPEIMD AIENEKTVHK TMSIYNVDRS VCGRIAGVIA KKYGDTGFAG
1410 1420 1430 1440 1450
QLNLTFTGSA GQSFACFLTP GMNIRLVGEA NDYVGKGMAG GEVVILPVES
1460 1470 1480 1490 1500
TGFRPEDATI VGNTCLYGAT GGLLFVRGKA GERFAVRNSL AQAVVEGTGD
1510 1520 1530 1540 1550
HCCEYMTGGC VVILGKVGRN VAAGMTGGLA YILDEDNTLL PKMNKEIVKI
1560 1570 1580 1590 1600
QRVTSPVGQT QLKSLIQAHV EKTGSSKGAM IVEEWDKYLA MFWQLVPPSE
1610 1620
EDTPEANSDH ILKTTTGDEE QVSSTLAEK
Length:1,629
Mass (Da):177,752
Last modified:July 13, 2010 - v2
Checksum:i83B02D81807F2DC7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861S → P in AAC78552 (PubMed:9596633).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39288 mRNA. Translation: AAC78552.1.
AC005662 Genomic DNA. Translation: AAC78549.1.
CP002685 Genomic DNA. Translation: AEC09945.1.
PIRiC84839.
RefSeqiNP_181655.1. NM_129687.4.
UniGeneiAt.21033.

Genome annotation databases

EnsemblPlantsiAT2G41220.1; AT2G41220.1; AT2G41220.
GeneIDi818721.
GrameneiAT2G41220.1; AT2G41220.1; AT2G41220.
KEGGiath:AT2G41220.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39288 mRNA. Translation: AAC78552.1.
AC005662 Genomic DNA. Translation: AAC78549.1.
CP002685 Genomic DNA. Translation: AEC09945.1.
PIRiC84839.
RefSeqiNP_181655.1. NM_129687.4.
UniGeneiAt.21033.

3D structure databases

ProteinModelPortaliQ9T0P4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4058. 1 interaction.
STRINGi3702.AT2G41220.1.

PTM databases

iPTMnetiQ9T0P4.

Proteomic databases

PaxDbiQ9T0P4.
PRIDEiQ9T0P4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G41220.1; AT2G41220.1; AT2G41220.
GeneIDi818721.
GrameneiAT2G41220.1; AT2G41220.1; AT2G41220.
KEGGiath:AT2G41220.

Organism-specific databases

TAIRiAT2G41220.

Phylogenomic databases

eggNOGiKOG0399. Eukaryota.
COG0067. LUCA.
COG0069. LUCA.
COG0070. LUCA.
HOGENOMiHOG000031558.
InParanoidiQ9T0P4.
KOiK00284.
OMAiHGRENDI.
PhylomeDBiQ9T0P4.

Enzyme and pathway databases

UniPathwayiUPA00045.
UPA00634; UER00691.
BioCyciARA:AT2G41220-MONOMER.
BRENDAi1.4.7.1. 399.

Miscellaneous databases

PROiQ9T0P4.

Gene expression databases

GenevisibleiQ9T0P4. 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. "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], TISSUE SPECIFICITY, FUNCTION.
    Strain: cv. Columbia.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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, DISRUPTION PHENOTYPE, FUNCTION.
  5. "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.

Entry informationi

Entry nameiGLTB2_ARATH
AccessioniPrimary (citable) accession number: Q9T0P4
Secondary accession number(s): O80665
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: July 13, 2010
Last modified: February 17, 2016
This is version 137 of the entry and version 2 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.