[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=K12; DOI=10.1016/0378-1119(87)90207-1; PubMed=3326786 [NCBI, ExPASy, EBI, Israel, Japan] Oliver G., Gosset G., Sanchez-Pescador R., Lozoya E., Ku L.M., Flores N., Becerril B., Valle F., Bolivar F.; "Determination of the nucleotide sequence for the glutamate synthase structural genes of Escherichia coli K-12."; Gene 60:1-11(1987).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[4]	PROTEIN SEQUENCE OF 2-13. STRAIN=K12 / EMG2; DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan] Link A.J., Robison K., Church G.M.; "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."; Electrophoresis 18:1259-1313(1997).
[5]	PROTEIN SEQUENCE OF 2-5. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1006/jmbi.1998.1726; PubMed=9600841 [NCBI, ExPASy, EBI, Israel, Japan] Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.; "Protein identification with N and C-terminal sequence tags in proteome projects."; J. Mol. Biol. 278:599-608(1998).
[6]	DISCUSSION OF SEQUENCE. PubMed=2643092 [NCBI, ExPASy, EBI, Israel, Japan] Gosset G., Merino E., Recillas F., Oliver G., Becerril B., Bolivar F.; "Amino acid sequence analysis of the glutamate synthase enzyme from Escherichia coli K-12."; Protein Seq. Data Anal. 2:9-16(1989).

Comments

CATALYTIC ACTIVITY: 2 L-glutamate + NADP⁺ = L-glutamine + 2-oxoglutarate + NADPH.
COFACTOR: Binds 1 4Fe-4S cluster.
PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADPH route): step 1/1 .
PATHWAY: Energy metabolism; nitrogen metabolism .
SUBUNIT: Aggregate of 4 catalytic active heterodimers, consisting of a large and a small subunit.
INTERACTION:
P09831:gltB; NbExp=2; IntAct=EBI-544293, EBI-551179;
MISCELLANEOUS: Glutamine binds to the large subunit and transfers the amido group to 2-oxo-glutamate that apparently binds to the small subunit.
SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M18747; AAA23905.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U18997; AAA58015.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76245.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77257.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

G65112; G65112.

RefSeq

AP_003756.1; -.
NP_417680.1; -.

3D structure databases

HSSP

Q28943; 1GTE. [HSSP ENTRY / PDB]

ModBase

P09832.

Protein-protein interaction databases

DIP

DIP:9803N; -.

IntAct

P09832; 6.

Enzyme and pathway databases

BioCyc

EcoCyc:GLUSYNSMALL-MON; -.
MetaCyc:GLUSYNSMALL-MON; -.

2D gel databases

SWISS-2DPAGE

P09832; -.

ECO2DBASE

F050.4; 6TH EDITION.

Organism-specific databases

EchoBASE

EB0399; -.

EcoGene

EG10404; gltD.

Ontologies

GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0004355;	Molecular function: glutamate synthase (NADPH) activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006537;	Biological process: glutamate biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000759; Adrndx_reductase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR012285; Fum_reductase_C.
IPR006006; Glut_synth_sub2.
IPR001327; Pyr_OxRdtase_NAD_bd.
IPR000103; Pyridine_nuc-diS_OxRdtase_2.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.1060.10; Fum_reductase_C; 1.

Pfam

PF00070; Pyr_redox; 2.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00469; PNDRDTASEII.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01318; gltD_gamma_fam; 1.

PROSITE

PS51379; 4FE4S_FER_2; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

947723; -.

GenomeReviews

AP009048_GR; JW3180.
U00096_GR; b3213.

KEGG

ecj:JW3180; -.
eco:b3213; -.

Phylogenomic databases

HOGENOM

P09832; -.

Genome annotation databases

CMR

P09832; b3213.

Other

ProtoNet

P09832.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

4Fe-4S; Amino-acid biosynthesis; Complete proteome; Direct protein sequencing; Glutamate biosynthesis; Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 472`	`471`	`Glutamate synthase [NADPH] small chain.`	`PRO_0000170800`
`DOMAIN`	`38 69`	`32`	`4Fe-4S ferredoxin-type.`
`METAL`	`94 94`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`98 98`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`104 104`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`108 108`		`Iron-sulfur (4Fe-4S) (Potential).`
`CONFLICT`	`38 51`		`GQAKAQADRCLSCG -> ARPKRRLTAACRAA (in Ref. 1).`
`CONFLICT`	`123 123`		`E -> K (in Ref. 1; AAA23905).`
`CONFLICT`	`174 174`		`V -> C (in Ref. 1; AAA23905).`
`CONFLICT`	`257 270`		`VYAALPFLIANTKQ -> CTQRCRSSSPTPNS (in Ref. 1).`
`CONFLICT`	`312 313`		`KH -> ND (in Ref. 1; AAA23905).`
`CONFLICT`	`376 400`		`GRRRAEIVAGSEHIVPADAVIMAFG -> ASPRGDRCRFRTYRTGRCGDHGVW (in Ref. 1; AAA23905).`

Sequence information

Length: 472 AA [This is the length of the unprocessed precursor]

Molecular weight: 52015 Da [This is the MW of the unprocessed precursor]

CRC64: F188CE1086040433 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSQNVYQFID LQRVDPPKKP LKIRKIEFVE IYEPFSEGQA KAQADRCLSC GNPYCEWKCP 

        70         80         90        100        110        120 
VHNYIPNWLK LANEGRIFEA AELSHQTNTL PEVCGRVCPQ DRLCEGSCTL NDEFGAVTIG 

       130        140        150        160        170        180 
NIERYINDKA FEMGWRPDMS GVKQTGKKVA IIGAGPAGLA CADVLTRNGV KAVVFDRHPE 

       190        200        210        220        230        240 
IGGLLTFGIP AFKLEKEVMT RRREIFTGMG IEFKLNTEVG RDVQLDDLLS DYDAVFLGVG 

       250        260        270        280        290        300 
TYQSMRGGLE NEDADGVYAA LPFLIANTKQ LMGFGETRDE PFVSMEGKRV VVLGGGDTAM 

       310        320        330        340        350        360 
DCVRTSVRQG AKHVTCAYRR DEENMPGSRR EVKNAREEGV EFKFNVQPLG IEVNGNGKVS 

       370        380        390        400        410        420 
GVKMVRTEMG EPDAKGRRRA EIVAGSEHIV PADAVIMAFG FRPHNMEWLA KHSVELDSQG 

       430        440        450        460        470 
RIIAPEGSDN AFQTSNPKIF AGGDIVRGSD LVVTAIAEGR KAADGIMNWL EV

P09832 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools