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Reviewed, UniProtKB/Swiss-Prot P27630 (PABB_STRLI)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Para-aminobenzoate synthase component 1
    EC=2.6.1.85
Alternative name(s):
    Para-aminobenzoate synthase component I
    ADC synthase
Gene names
Name: pabB
OrganismStreptomyces lividans
Taxonomic identifier1916 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 processFolate biosynthesis
   Molecular functionTransferase
Gene Ontology (GO)
   Biological processfolic acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function4-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 475475Para-aminobenzoate synthase component 1
PRO_0000154140

Sequences

Sequence LengthMass (Da)Tools
P27630-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 978A05EB35F2BEB3

FASTA47552,042
        10         20         30         40         50         60 
MASCRMGARS ALEPCQVDCL DEAADERCAE TPRCHAELLE SVTGASRMSR YSIIVLDPIG 

        70         80         90        100        110        120 
TIRAAEALTA LVDADDVIFK DEDPLKGIRS VFELGDLDPT NHEEIEFQGG ALGRFAYDIA 

       130        140        150        160        170        180 
RRLEAIRDLG DRELAGPDAG TALYDLILYD HQDDVIWILV PNEAGEQDPS EDFRDLVNAW 

       190        200        210        220        230        240 
SYDDEFDIGA EFGANYTDDA YADGVDRLKD YLGSGDMYQV NLAQRRVGMI SAEDYQLYIR 

       250        260        270        280        290        300 
LRDANPAPYM AYLDIDEGLL VASPERIILD EASDLDTRPI AGTLRGRPRA GGDDEDDGRA 

       310        320        330        340        350        360 
IDLLRVDKDR AERIMIVDLD RNDIARVGVG GSVKVREIMG LERYSGVMHL VSQVTGDLQE 

       370        380        390        400        410        420 
AIEAVDLIRA GFPGGTLTGA PKVRTMEIID ELEPQRRAAY CGSIGYIAYK GNIDFKIAIP 

       430        440        450        460        470 
TLYALAGQLF CQAGGGVVGD SVPDGEYRES FEKGNALIRG LEIRHGAVVA QSEDK 

« Hide

References

[1]"Organization of the genes encoding p-aminobenzoic acid synthetase from Streptomyces lividans 1326."
Arhin F.F., Vining L.C.
Gene 126:129-133(1993) [PubMed: 8472953] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 66 / 1326.
[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.

Cross-references

Sequence databases

M64859 Genomic DNA. Translation: AAA26798.1.
PIRJN0578.

3D structure databases

HSSPHSSP built from PDB template 1K0E based on UniProtKB P05041.
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.6.1.85. 15238.

Family and domain databases

InterProIPR005801. ADC_synthase.
IPR006805. Anth_synth_I_N.
IPR019999. Anthranilate_synth_I_C.
IPR015890. Chorismate-bd_C.
[Graphical view]
Gene3DG3DSA:3.60.120.10. TRPE_1_chor_bd. 1 hit.
PANTHERPTHR11236. TRPE_1_chor_bd. 1 hit.
PfamPF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view]
PRINTSPR00095. ANTSNTHASEI.
ProDomPD000779. Anth_synth_chor. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry namePABB_STRLI
AccessionPrimary (citable) accession number: P27630
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents