Reviewed, UniProtKB/Swiss-Prot P09832 (GLTD_ECOLI)

Names and origin

Protein names

Recommended name:
    Glutamate synthase [NADPH] small chain
    EC=1.4.1.13
Alternative name(s):
    Glutamate synthase subunit beta
      Short name=GLTS beta chain
    NADPH-GOGAT

Gene names

Name:	gltD
Synonyms:	aspB
Ordered Locus Names:	b3213, JW3180

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	472 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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. Energy metabolism; nitrogen metabolism.
Subunit structure	Aggregate of 4 catalytic active heterodimers, consisting of a large and a small subunit.
Miscellaneous	Glutamine binds to the large subunit and transfers the amido group to 2-oxo-glutamate that apparently binds to the small subunit.
Sequence similarities	Contains 1 4Fe-4S ferredoxin-type domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Glutamate biosynthesis
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glutamate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro glutamate synthase (NADPH) activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
gltB	P09831	2	EBI-544293,EBI-551179

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4 Ref.5
	Chain	2 – 472	471	Glutamate synthase [NADPH] small chain		PRO_0000170800
Regions
	Domain	38 – 69	32	4Fe-4S ferredoxin-type
Sites
	Metal binding	94	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	98	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	104	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	108	1	Iron-sulfur (4Fe-4S) Potential
Experimental info
	Sequence conflict	38 – 51	14	GQAKA…CLSCG → ARPKRRLTAACRAA Ref.1
	Sequence conflict	123	1	E → K in AAA23905. Ref.1
	Sequence conflict	174	1	V → C in AAA23905. Ref.1
	Sequence conflict	257 – 270	14	VYAAL…ANTKQ → CTQRCRSSSPTPNS Ref.1
	Sequence conflict	312 – 313	2	KH → ND in AAA23905. Ref.1
	Sequence conflict	376 – 400	25	GRRRA…IMAFG → ASPRGDRCRFRTYRTGRCGD HGVW in AAA23905. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P09832-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F188CE1086040433	FASTA	472	52,015
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Determination of the nucleotide sequence for the glutamate synthase structural genes of Escherichia coli K-12." Oliver G., Gosset G., Sanchez-Pescador R., Lozoya E., Ku L.M., Flores N., Becerril B., Valle F., Bolivar F. Gene 60:1-11(1987) [PubMed: 3326786] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: K12.
[2]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[5]	"Protein identification with N and C-terminal sequence tags in proteome projects." 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. J. Mol. Biol. 278:599-608(1998) [PubMed: 9600841] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Amino acid sequence analysis of the glutamate synthase enzyme from Escherichia coli K-12." Gosset G., Merino E., Recillas F., Oliver G., Becerril B., Bolivar F. Protein Seq. Data Anal. 2:9-16(1989) [PubMed: 2643092] [Abstract] Cited for: DISCUSSION OF SEQUENCE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M18747 Genomic DNA. Translation: AAA23905.1. U18997 Genomic DNA. Translation: AAA58015.1. U00096 Genomic DNA. Translation: AAC76245.1. AP009048 Genomic DNA. Translation: BAE77257.1.
PIR	G65112.
RefSeq	AP_003756.1. NP_417680.1.
3D structure databases
HSSP	HSSP built from PDB template 1GTE based on UniProtKB Q28943.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:9803N.
IntAct	P09832. 6 interactions.
2-D gel databases
SWISS-2DPAGE	P09832.
ECO2DBASE	F050.4. 6TH EDITION.
Genome annotation databases
GeneID	947723.
GenomeReviews	Gene locus JW3180 in contig AP009048_GR. Gene locus b3213 in contig U00096_GR.
KEGG	ecj:JW3180. eco:b3213.
Organism-specific databases
EchoBASE	EB0399.
EcoGene	EG10404. gltD.
CMR	Search...
Phylogenomic databases
HOGENOM	P09832.
OMA	P09832. DMSKVEW.
Enzyme and pathway databases
BioCyc	EcoCyc:GLUSYNSMALL-MON. MetaCyc:GLUSYNSMALL-MON.
BRENDA	1.4.1.13. 246.
Family and domain databases
InterPro	IPR017896. 4Fe4S_Fe-S-bd. IPR000759. Adrndx_reductase. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR012285. Fum_reductase_C. IPR006006. Glut_synth_sub2. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
Gene3D	G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.
Pfam	PF00070. Pyr_redox. 2 hits. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PRINTS	PR00419. ADXRDTASE.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01318. gltD_gamma_fam. 1 hit.
PROSITE	PS51379. 4FE4S_FER_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLTD_ECOLI

Accession

Primary (citable) accession number: P09832
Secondary accession number(s): Q2M8Z9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)