P12679 (PABB_ENTAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Para-aminobenzoate synthase component 1
EC=2.6.1.85

Alternative name(s):
ADC synthase
Para-aminobenzoate synthase component I

Gene names

Name:

pabB

Organism

Enterobacter aerogenes (Aerobacter aerogenes)

Taxonomic identifier

548 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Enterobacter

Protein attributes

Sequence length	451 AA.
Sequence status	Complete.
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	Belongs to the anthranilate synthase component I family.

Ontologies

Keywords
Biological process	Folate biosynthesis
Molecular function	Transferase
Gene Ontology (GO)
Biological process	folic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4-amino-4-deoxychorismate synthase activity Inferred from electronic annotation. Source: EC oxo-acid-lyase 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 – 451	451	Para-aminobenzoate synthase component 1		PRO_0000154137

Sequences

	Sequence		Length	Mass (Da)
	P12679 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 952C6887158E228C	FASTA	451	50,363
	10 20 30 40 50 60 MLSPAMISLP WRPDAAEYYF SPLSSQPWAM LLHSGFAEHA HNRFDIIVAQ PRATLVTHGQ 70 80 90 100 110 120 LTTLREGETV STSAADPLTL VHQQLAHCNL QPQPHPHLPF LGGALGLFGY DLGRRFEHLP 130 140 150 160 170 180 ARADADIELP DMAVGIYDWA LIVDHQRREV SLFSYDDPQA RLAWLEAQTA PVAATFTLTS 190 200 210 220 230 240 AWRANMSREE YGEKFRQIQA YLHSGDCYQV NLAQRFTATY RGDEWQAFRQ LNRANRAPFS 250 260 270 280 290 300 AFIRLDEGAV LSLSPERFIQ LRQGDIQTRP IKGTLPRLAD PEQDALQQQK LANSPKDRAE 310 320 330 340 350 360 NLMIVDLMRN DIGRVAEPGS VRVPELFVVE PFPAVHHLVS TVTARLPAHL HAADLLRAAF 370 380 390 400 410 420 PGGSITGAPK VRAMEIIDEL EPQRRNAWCG SIGYLSFCGN MDSSITIRTL TAWQGHLYCS 430 440 450 AGGGIVADSE EAAEYQETFD KVNRILHQLE S

References

[1]	"Evolution of aminobenzoate synthases: nucleotide sequences of Salmonella typhimurium and Klebsiella aerogenes pabB." Goncharoff P., Nichols B.P. Mol. Biol. Evol. 5:531-548(1988) [PubMed: 3057324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"p-aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase." Ye Q.-Z., Liu J., Walsh C.T. Proc. Natl. Acad. Sci. U.S.A. 87:9391-9395(1990) [PubMed: 2251281] [Abstract] Cited for: CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M22078 Genomic DNA. Translation: AAA88207.1.
3D structure databases
ProteinModelPortal	P12679.
SMR	P12679. Positions 2-450.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR005801. ADC_synthase. IPR019999. Anth_synth_I. IPR006805. Anth_synth_I_N. IPR015890. Chorismate-bd_C. IPR005802. Para-NH2Bz_synth_comp_1. [Graphical view]
Gene3D	G3DSA:3.60.120.10. TRPE_1_chor_bd. 1 hit.
Pfam	PF04715. Anth_synt_I_N. 1 hit. PF00425. Chorismate_bind. 1 hit. [Graphical view]
PRINTS	PR00095. ANTSNTHASEI.
SUPFAM	SSF56322. TRPE_1_chor_bd. 1 hit.
TIGRFAMs	TIGR00553. PabB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PABB_ENTAE

Accession

Primary (citable) accession number: P12679

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	June 28, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program