Reviewed, UniProtKB/Swiss-Prot Q05542 (GLNA1_STRVR)

Names and origin

Protein names

Recommended name:
    Glutamine synthetase 1
    EC=6.3.1.2
Alternative name(s):
    Glutamine synthetase I
      Short name=GSI
    Glutamate--ammonia ligase I

Gene names

Name:	glnI
Synonyms:	glnA

Organism

Streptomyces viridochromogenes

Taxonomic identifier

1938 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	469 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.
Enzyme regulation	The activity of this enzyme is controlled by adenylation under conditions of abundant glutamine. The fully adenylated enzyme complex is inactive By similarity.
Subunit structure	Oligomer of 12 subunits arranged in the form of two hexagons.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the glutamine synthetase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Gene Ontology (GO)
Biological process	glutamine biosynthetic process Inferred from electronic annotation. Source: InterPro nitrogen fixation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate-ammonia ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 469	469	Glutamine synthetase 1		PRO_0000153269
Amino acid modifications
	Modified residue	397	1	O-AMP-tyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q05542-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 2F152E5A5A4283E4	FASTA	469	52,248
	10 20 30 40 50 60 MFQNADEAKK LIADEDVKFI DVRFCDLPGV MQHFTIPASA FDPAEELAFD GSSIRGFQAI 70 80 90 100 110 120 HESDMAVRAD LSTARVDPFR RDKTVNINFF IHDPITGEQY SRDPRNVAKK AEAYLASTGI 130 140 150 160 170 180 GDTGYFGPEA EFYVFDSVRL ANSATESFYH IDSEAGAWNT GALENNRGYK VRYKGGYFPV 190 200 210 220 230 240 PPVDHFADLR AQISLELDRA GLQVERHDHE VGTAGQAEIN YKFNTLLAAA DDLQLFKYIV 250 260 270 280 290 300 KNVAWQNGKT ATFMPKPIFG DNGSGMHVHQ SLWTGGQALF YDEAGYAGLS DTARYYMGGI 310 320 330 340 350 360 LKHAPSLLAF TNPTVNSYHR LVPGFEAPVN LVYSQRNRSA AMRIPITGSN PKAKRVEFRA 370 380 390 400 410 420 PDSSGNPYLA FSALLLAGLD GIKNKIEPAE PIDKDLYELA PEEHAGVPQV PTSLPAVLDR 430 440 450 460 LEADHEFLLA GDVFTPDLIE TWIDYKRTNE IAPLQLRPHP YEYEQYYDV

References

[1]

"Evolution of the glutamine synthetase gene, one of the oldest existing and functioning genes." Kumada Y., Benson D.R., Hillemann D., Hosted T.J., Rocheford D.A., Thompson C.J., Wohlleben W., Tateno Y. Proc. Natl. Acad. Sci. U.S.A. 90:3009-3013(1993) [PubMed: 8096645] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	X70924 Genomic DNA. Translation: CAA50272.1.
PIR	S32024.
3D structure databases
HSSP	HSSP built from PDB template 1LGR based on UniProtKB P06201.
ModBase	Search...
Enzyme and pathway databases
BRENDA	6.3.1.2. 39938.
Family and domain databases
InterPro	IPR008147. Gln_synt_beta. IPR014746. Gln_synth/guanido_kin_cat. IPR008146. Gln_synth_cat. IPR004809. Gln_synth_I. IPR001637. Gln_synth_I_adenyltn_S. [Graphical view]
Gene3D	G3DSA:3.30.590.10. ATP-gua_Ptrans. 1 hit.
Pfam	PF00120. Gln-synt_C. 1 hit. PF03951. Gln-synt_N. 1 hit. [Graphical view]
ProDom	PD001057. Gln_synt_C. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00653. GlnA. 1 hit.
PROSITE	PS00180. GLNA_1. 1 hit. PS00182. GLNA_ADENYLATION. 1 hit. PS00181. GLNA_ATP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLNA1_STRVR

Accession

Primary (citable) accession number: Q05542

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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