P00900 (TRPG_SERMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Anthranilate synthase component II
EC=4.1.3.27

Alternative name(s):
Glutamine amido-transferase

Gene names

Name:

trpG

Organism

Serratia marcescens

Taxonomic identifier

615 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Serratia

Protein attributes

Sequence length	193 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	Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
Subunit structure	Tetramer of two components I and two components II.
Miscellaneous	Component I catalyzes the formation of anthranilate using ammonia rather than glutamine, whereas component II provides glutamine amidotransferase activity.
Sequence similarities	Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tryptophan biosynthesis
Domain	Glutamine amidotransferase
Molecular function	Lyase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW tryptophan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	anthranilate synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
trpE	P00897	2	EBI-1031352,EBI-1031345

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2 Ref.3

Chain

2 – 193

192

Anthranilate synthase component II

PRO_0000056898

Regions

Domain

3 – 193

191

Glutamine amidotransferase type-1

Sites

Active site

84

1

Active site

170

1

By similarity

Active site

172

1

By similarity

Experimental info

Sequence conflict

36

1

G → A AA sequence Ref.2

Sequence conflict

38

1

E → Q AA sequence Ref.2

Sequence conflict

38

1

E → Q AA sequence Ref.3

Sequence conflict

45

1

Q → E AA sequence Ref.2

Sequence conflict

46

1

H → Q AA sequence Ref.3

Sequence conflict

48

1

E → T AA sequence Ref.2

Sequence conflict

60 – 62

3

TPS → ASV AA sequence Ref.3

Sequence conflict

77

1

Q → R AA sequence Ref.2

Sequence conflict

150

1

S → F AA sequence Ref.2

Secondary structure

1

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193

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

14 – 23

10

Beta strand

27 – 32

6

Helix

37 – 46

10

Beta strand

48 – 54

7

Helix

61 – 63

3

Helix

67 – 74

8

Turn

75 – 77

3

Beta strand

80 – 83

4

Helix

85 – 93

9

Beta strand

97 – 114

18

Helix

118 – 120

3

Beta strand

125 – 139

15

Beta strand

144 – 150

7

Beta strand

153 – 159

7

Turn

160 – 163

4

Beta strand

164 – 169

6

Helix

179 – 191

13

Sequences

	Sequence		Length	Mass (Da)
	P00900 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 8F53EBFEC7F4524A	FASTA	193	20,868
	10 20 30 40 50 60 MADILLLDNV DSFTYNLVDQ LRASGHQVVI YRNQIGAEVI IERLQHMEQP VLMLSPGPGT 70 80 90 100 110 120 PSEAGCMPEL LQRLRGQLPI IGICLGHQAI VEAYGGQVGQ AGEILHGKAS AIAHDGEGMF 130 140 150 160 170 180 AGMANPLPVA RYHSLVGSNI PADLTVNARS GEMVMAVRDD RRRVCGFQFH PESILTTHGA 190 RLLEQTLAWA LAK

References

[1]	"Nucleotide sequences of the trpG regions of Escherichia coli, Shigella dysenteriae, Salmonella typhimurium and Serratia marcescens." Nichols B.P., Miozzari G.F., van Cleemput M., Bennett G.N., Yanofsky C. J. Mol. Biol. 142:503-517(1980) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Primary structure of Serratia marcescens anthranilate synthase component II." Tso J.Y., Hermodson M.A., Zalkin H. J. Biol. Chem. 255:1451-1457(1980) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-193.
[3]	"Separation of anthranilate synthetase components I and II of Escherichia coli, Salmonella typhimurium, and Serratia marcescens and determination of their amino-terminal sequences by automatic Edman degradation." Li S.-L., Hanlon J., Yanofsky C. Biochemistry 13:1736-1744(1974) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-62.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY027546 Genomic DNA. Translation: AAK37409.1.

PIR

NNSE2. D92860.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I7Q	X-ray	1.95	B/D	1-193	[»]
1I7S	X-ray	2.40	B/D	1-193	[»]

ProteinModelPortal

P00900.

SMR

P00900. Positions 2-193.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00900. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00035; UER00040.

Family and domain databases

InterPro

IPR017926. GATASE.
IPR006221. TrpG/PapA_dom.
[Graphical view]

Pfam

PF00117. GATase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00566. trpG_papA. 1 hit.

PROSITE

PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00900.

Entry information

Entry name

TRPG_SERMA

Accession

Primary (citable) accession number: P00900

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program