Q9T0P4 (GLTB2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ferredoxin-dependent glutamate synthase 2, chloroplastic
EC=1.4.7.1

Alternative name(s):
Fd-GOGAT 2

Gene names

Name:	GLU2
Ordered Locus Names:	At2g41220
ORF Names:	F13H10.23

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	1629 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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. Ref.1 Ref.4
Catalytic activity	2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+.
Cofactor	Binds 1 3Fe-4S cluster By similarity. FAD By similarity. FMN By similarity.
Pathway	Amino-acid biosynthesis; L-glutamate biosynthesis via GLT pathway; L-glutamate from 2-oxoglutarate and L-glutamine (ferredoxin route): step 1/1. Energy metabolism; nitrogen metabolism.
Subcellular location	Plastid › chloroplast stroma By similarity.
Tissue specificity	Expressed predominantly in roots and slightly in leaves. Low expression in the leaf mesophyll and phloem companion cell-sieve element complex. Ref.1 Ref.4
Disruption phenotype	No visible phenotype. The glutamate and glutamine levels were unaffected. Ref.4
Sequence similarities	Belongs to the glutamate synthase family. Contains 1 glutamine amidotransferase type-2 domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Glutamate biosynthesis
Cellular component	Chloroplast Plastid
Domain	Glutamine amidotransferase Transit peptide
Ligand	3Fe-4S FAD FMN Flavoprotein Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-glutamate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chloroplast envelope Inferred from direct assay PubMed 12938931. Source: TAIR chloroplast stroma Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate synthase (ferredoxin) activity Inferred from sequence or structural similarity Ref.1. Source: TAIR metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 107	107	Chloroplast By similarity
	Chain	108 – 1629	1522	Ferredoxin-dependent glutamate synthase 2, chloroplastic		PRO_0000011615
Regions
	Domain	108 – 507	400	Glutamine amidotransferase type-2
	Nucleotide binding	1186 – 1243	58	FMN By similarity
Sites
	Active site	108	1	For GATase activity By similarity
	Metal binding	1239	1	Iron-sulfur (3Fe-4S) By similarity
	Metal binding	1245	1	Iron-sulfur (3Fe-4S) By similarity
	Metal binding	1250	1	Iron-sulfur (3Fe-4S) By similarity
Experimental info
	Sequence conflict	86	1	S → P in AAC78552. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9T0P4 [UniParc]. Last modified July 13, 2010. Version 2. Checksum: 83B02D81807F2DC7	FASTA	1,629	177,752
	10 20 30 40 50 60 MALQSPGATG ASSSVSRLLS SAKLSSTKTI FSVDFVRSYC ISKGTKRRNE LSGFRGYSPL 70 80 90 100 110 120 LKSSLRSPFS VKAILNSDRA AGDASSSFSD LKPQVAYLED IISERGACGV GFIANLENKA 130 140 150 160 170 180 THKIVNDALI ALGCMEHRGG CGSDNTSGDG SGLMTSIPWD LFNEWAEKQG IASFDRTHTG 190 200 210 220 230 240 VGMLFLPRDD NIRKEAKKVI TSIFEKEGLE VLGWRDVPVE ASIVGHNAKQ TMPNTEQVFV 250 260 270 280 290 300 RIVKDDKVDD VERELYICRK LIERAVASES WASELYFSSL SNQTIVYKGM LRSEVLGLFY 310 320 330 340 350 360 PDLQNDLYKS PFAIYHRRFS TNTSPRWHLA QPMRFLGHNG EINTIQGNLN WMTSREASLR 370 380 390 400 410 420 SPVWHGREND IRPISNPKAS DSANLDSAAE LLIRSGRTPE ESLMILVPEA YKNHPTLMIK 430 440 450 460 470 480 YPEAVDFYDY YKGQMEPWDG PALVLFSDGK TVGACLDRNG LRPARYWRTS DNVVYVASEV 490 500 510 520 530 540 GVLPMDESKV TMKGRLGPGM MISVDLENGQ VYENTEVKKR VASYNPYGKW VSENLRNLKP 550 560 570 580 590 600 SNYLSSAILE TDETLRRQQA FGYSSEDVQM VIESMAAQGK EPTFCMGDDT PVAVLSQKPH 610 620 630 640 650 660 MLYDYFKQRF AQVTNPAIDP LREGLVMSLE VNIGKRGNIL EVGPQNVSQV VLSGPVLNER 670 680 690 700 710 720 ELEGLLGDPL LKSQILPTFF DIRRGIEGSL KKGLLKLCEA ADEAVRNGSQ VLVLSDRSDN 730 740 750 760 770 780 PEPTRPAIPM LLAVGAVHQH LIQNGLRMSA SIIADTAQCF STHHFACLIG YGASAICPHL 790 800 810 820 830 840 ALETCRQWRL SNKTVNMMRN GKMPTVTMEQ AQKNYRKAVN TGLLKVLSKM GISLFSSYCG 850 860 870 880 890 900 AQIFEIYGLG NEVVEFSFRG SASQIGGLTL DELARETLTF WVRAFSEDTA KRLENFGFIQ 910 920 930 940 950 960 FRPGGEYHGN NPEMSKLLHK AVREKSETAY AVYQQHLANR PITVFRDLLE FKSDRNPIPV 970 980 990 1000 1010 1020 GKVEPASSIV ERFCTGGMSL GAISRETHET IAIAMNRLGG KSNSGEGGED PIRWKPLTDV 1030 1040 1050 1060 1070 1080 VDGYSSTLPH LKGLRNGDTA TSAIKQVASG RFGVTPTFLV NADQLEIKVA QGAKPGEGGQ 1090 1100 1110 1120 1130 1140 LPGKKVSAYI ARLRNSKPGV PLISPPPHHD IYSIEDLAQL IFDLHQVNPK AKVSVKLVSE 1150 1160 1170 1180 1190 1200 TGIGTVASGV AKANADIIQI SGYDGGTGAS PISSIKHAGG PWELGLAETQ KTLIGNGLRE 1210 1220 1230 1240 1250 1260 RVIIRVDGGF KSGVDVLIAA AMGADEYGFG TLAMIATGCI MARICHTNNC PVGVASQREE 1270 1280 1290 1300 1310 1320 LRARFPGLPG DLVNFFLYIA EEVRGILAQL GYEKLDDIIG RTDLLKARDI SLVKTHLDLS 1330 1340 1350 1360 1370 1380 YLLSSVGLPK RSSTSIRKQE VHSNGPVLDD TLLQDPEIMD AIENEKTVHK TMSIYNVDRS 1390 1400 1410 1420 1430 1440 VCGRIAGVIA KKYGDTGFAG QLNLTFTGSA GQSFACFLTP GMNIRLVGEA NDYVGKGMAG 1450 1460 1470 1480 1490 1500 GEVVILPVES TGFRPEDATI VGNTCLYGAT GGLLFVRGKA GERFAVRNSL AQAVVEGTGD 1510 1520 1530 1540 1550 1560 HCCEYMTGGC VVILGKVGRN VAAGMTGGLA YILDEDNTLL PKMNKEIVKI QRVTSPVGQT 1570 1580 1590 1600 1610 1620 QLKSLIQAHV EKTGSSKGAM IVEEWDKYLA MFWQLVPPSE EDTPEANSDH ILKTTTGDEE QVSSTLAEK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U39288 mRNA. Translation: AAC78552.1. AC005662 Genomic DNA. Translation: AAC78549.1. CP002685 Genomic DNA. Translation: AEC09945.1.
IPI	IPI00533390.
PIR	C84839.
RefSeq	NP_181655.1. NM_129687.4.
UniGene	At.21033.
3D structure databases
ProteinModelPortal	Q9T0P4.
ModBase	Search...
Proteomic databases
PaxDb	Q9T0P4.
PRIDE	Q9T0P4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G41220.1; AT2G41220.1; AT2G41220.
GeneID	818721.
KEGG	ath:AT2G41220.
Organism-specific databases
TAIR	At2g41220.
Phylogenomic databases
eggNOG	COG0069.
HOGENOM	HOG000031558.
InParanoid	Q9T0P4.
KO	K00284.
OMA	VNFFLYI.
PhylomeDB	Q9T0P4.
ProtClustDB	CLSN2913236.
Enzyme and pathway databases
UniPathway	UPA00045. UPA00634; UER00691.
Gene expression databases
Genevestigator	Q9T0P4.
GermOnline	AT2G41220. Arabidopsis thaliana.
Family and domain databases
Gene3D	2.160.20.60. 1 hit. 3.20.20.70. 2 hits.
InterPro	IPR013785. Aldolase_TIM. IPR017932. GATase_2_dom. IPR000583. GATase_dom. IPR002489. Glu_synth_asu_C. IPR002932. Glu_synth_centr_C. IPR006982. Glu_synth_centr_N. [Graphical view]
Pfam	PF00310. GATase_2. 1 hit. PF04898. Glu_syn_central. 1 hit. PF01645. Glu_synthase. 1 hit. PF01493. GXGXG. 1 hit. [Graphical view]
SUPFAM	SSF69336. Glu_synthase_C. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLTB2_ARATH

Accession

Primary (citable) accession number: Q9T0P4
Secondary accession number(s): O80665

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	July 13, 2010
Last modified:	May 29, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program