Reviewed, UniProtKB/Swiss-Prot P00903 (PABA_ECOLI)

Names and origin

Protein names

Recommended name:
    Para-aminobenzoate synthase glutamine amidotransferase component II
    EC=2.6.1.85
Alternative name(s):
    ADC synthase

Gene names

Name:	pabA
Ordered Locus Names:	b3360, JW3323

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	187 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC) from chorismate and glutamine.
Catalytic activity	Chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-aminobenzoate from chorismate: step 1/2.
Subunit structure	Consists of two non-identical chains: component I catalyzes the formation of ADC by binding chorismate and ammonia; component II provides the glutamine amidotransferase activity.
Sequence similarities	Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
Biological process	Folate biosynthesis
Domain	Glutamine amidotransferase
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	folic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4-amino-4-deoxychorismate synthase activity Inferred from electronic annotation. Source: EC anthranilate synthase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 187	187	Para-aminobenzoate synthase glutamine amidotransferase component II		PRO_0000056849
Regions
	Domain	1 – 187	187	Glutamine amidotransferase type-1
Sites
	Active site	79	1
	Active site	168	1
	Active site	170	1
Experimental info
	Mutagenesis	79	1	C → S: 10000-fold decrease in catalytic efficiency. Ref.6
	Mutagenesis	168	1	H → Q: Loss of activity. Ref.6
	Mutagenesis	170	1	E → A: 150-fold decrease in catalytic efficiency. Ref.6
	Mutagenesis	170	1	E → D: 4-fold decrease in catalytic efficiency. Ref.6
	Mutagenesis	170	1	E → K or Q: Loss of activity. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P00903-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 0E5F43499D5F55C6	FASTA	187	20,772
	10 20 30 40 50 60 MILLIDNYDS FTWNLYQYFC ELGADVLVKR NDALTLADID ALKPQKIVIS PGPCTPDEAG 70 80 90 100 110 120 ISLDVIRHYA GRLPILGVCL GHQAMAQAFG GKVVRAAKVM HGKTSPITHN GEGVFRGLAN 130 140 150 160 170 180 PLTVTRYHSL VVEPDSLPAC FDVTAWSETR EIMGIRHRQW DLEGVQFHPE SILSEQGHQL LANFLHR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of Escherichia coli pabA and its evolutionary relationship to trp(G)D." Kaplan J.B., Nichols B.P. J. Mol. Biol. 168:451-468(1983) [PubMed: 6350604] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Chromosomal organization and expression of Escherichia coli pabA." Tran P.V., Bannor T.A., Doktor S.Z., Nichols B.P. J. Bacteriol. 172:397-410(1990) [PubMed: 2403545] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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.
[4]	"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.
[5]	"Nucleotide sequences of fic and fic-1 genes involved in cell filamentation induced by cyclic AMP in Escherichia coli." Kawamukai M., Matsuda H., Fujii W., Utsumi R., Komano T. J. Bacteriol. 171:4525-4529(1989) [PubMed: 2546924] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150.
[6]	"p-aminobenzoate synthesis in Escherichia coli: mutational analysis of three conserved amino acid residues of the amidotransferase PabA." Roux B., Walsh C.T. Biochemistry 32:3763-3768(1993) [PubMed: 8096767] [Abstract] Cited for: MUTAGENESIS OF CYS-79; HIS-168 AND GLU-170.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M28363 Genomic DNA. Translation: AAA23774.1. K00030 Genomic DNA. Translation: AAA24260.1. M32354 Genomic DNA. Translation: AAA24264.1. U18997 Genomic DNA. Translation: AAA58157.1. U00096 Genomic DNA. Translation: AAC76385.1. AP009048 Genomic DNA. Translation: BAE77930.1.
PIR	AGEC2. A01124.
RefSeq	AP_004429.1. NP_417819.1.
3D structure databases
HSSP	HSSP built from PDB template 1I1Q based on UniProtKB P00905.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:10433N.
STRING	P00903.
Genome annotation databases
GeneID	947873.
GenomeReviews	Gene locus JW3323 in contig AP009048_GR. Gene locus b3360 in contig U00096_GR.
KEGG	ecj:JW3323. eco:b3360.
Organism-specific databases
EchoBASE	EB0676.
EcoGene	EG10682. pabA.
CMR	Search...
Phylogenomic databases
HOGENOM	P00903.
OMA	YNVVQYL.
Enzyme and pathway databases
BioCyc	EcoCyc:PABASYN-COMPII-MON. MetaCyc:PABASYN-COMPII-MON.
Gene expression databases
Genevestigator	P00903.
Family and domain databases
InterPro	IPR006220. Anth_synthII. IPR001317. CarbamoylP_synth_GATase. IPR011702. GATASE. IPR017926. GATASE_1. IPR000991. GATase_class1_C. IPR006221. TrpG_papA. [Graphical view]
Pfam	PF00117. GATase. 1 hit. [Graphical view]
PRINTS	PR00097. ANTSNTHASEII. PR00099. CPSGATASE. PR00096. GATASE.
TIGRFAMs	TIGR00566. trpG_papA. 1 hit.
PROSITE	PS51273. GATASE_TYPE_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PABA_ECOLI

Accession

Primary (citable) accession number: P00903
Secondary accession number(s): Q2M726

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	November 3, 2009
This is version 88 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)