P12680 (PABB_SALTY) 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
Ordered Locus Names:	STM1824

Organism

Salmonella typhimurium

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	454 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
Technical term	Complete proteome Reference proteome
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 – 454	454	Para-aminobenzoate synthase component 1		PRO_0000154139

Sequences

	Sequence		Length	Mass (Da)
	P12680 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 430B3949B4904546	FASTA	454	50,979
	10 20 30 40 50 60 MMKTLSPTVI TLPWRPDAAE HYFAPVNHLP WAMLLHSGDA IHPYNRFDIL VADPVTTLTT 70 80 90 100 110 120 RAQETTVCTA RTTTVTLDDP LHVLQTQLEA LPFHPQPDPD LPFQGGALGL FGYDLGRRFE 130 140 150 160 170 180 ILPDTAARDI ALPDMAIGLY DWALIVDHQK QVVSLISYHD ADARYRWLTS QRAPTRTPFR 190 200 210 220 230 240 LTSAWQSNMT RCEYGEKFRQ VQAWLHSGDC YQVNLSQRFQ ASYEGDEWQA FERLNRANRA 250 260 270 280 290 300 PFSAFLRLHD GAILSLSPER FIQLENGHIQ TRPIKGTLPR LNDPQADRQQ AQKLANSMKD 310 320 330 340 350 360 RAENLMIVDL MRNDIGRVAV PGSVKVPELF VVEPFPAVHH LVSTITARLP DSLHATDLLR 370 380 390 400 410 420 AAFPGGSITG APKVRAMEII DELEPQRRNA WCGSIGYLSF CGKMDTSITI RTVTATQGQL 430 440 450 YCSAGGGIVA DSNEEAEYQE TFDKVNRILH PLEN

References

	« Hide 'large scale' referencesShow 'large scale' 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]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"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	M22079 Genomic DNA. Translation: AAA88618.1. AE006468 Genomic DNA. Translation: AAL20739.1.
PIR	A31132.
RefSeq	NP_460780.1. NC_003197.1.
3D structure databases
ProteinModelPortal	P12680.
SMR	P12680. Positions 4-453.
ModBase	Search...
Proteomic databases
PRIDE	P12680.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1253343.
GenomeReviews	Gene locus STM1824 in contig AE006468_GR.
KEGG	stm:STM1824.
NMPDR	fig|99287.1.peg.1765.
PATRIC	32382171. VBISalEnt20916_1924.
Phylogenomic databases
HOGENOM	HBG507440.
OMA	HNRFDIL.
ProtClustDB	PRK15465.
Enzyme and pathway databases
BioCyc	STYP99287:STM1824-MONOMER.
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.
KO	K01665.
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_SALTY

Accession

Primary (citable) accession number: P12680

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program