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P27629 (PABB_LACLL) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismLactococcus lactis subsp. lactis (Streptococcus lactis)
Taxonomic identifier1360 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length470 AA.
Sequence statusComplete.
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 – 470470Para-aminobenzoate synthase component 1
PRO_0000154138

Sequences

Sequence LengthMass (Da)Tools
P27629 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: D2B50CD11A467817

FASTA47050,970
        10         20         30         40         50         60 
MFTISGVVLI TRPVYDEGSL NYCQSGAMNN GILLESVEGN KPRYSIGGAE PIGTINANAV 

        70         80         90        100        110        120 
LTAATYAEDV KFTDADPLNG TRVAICNGED TQQEEMGFQG GALGYFAYDV GRRLEGYNDL 

       130        140        150        160        170        180 
GIEDWAIPDL AGSSYEIGVS ADHQNDVIVL IAHASADGND VFITSSRQLS MVAGPTCCAS 

       190        200        210        220        230        240 
GDVEILRNKL HYYGVIPFSQ DDCGFNRLKD YLGSGDMYQV NLGNRNVGAI VMTLFQGYNQ 

       250        260        270        280        290        300 
LRLMNPGPYM VFLDEANIIM ASPEIVLADE ANDLNTRPIA GTLMRLNEQD EDGVNAACLG 

       310        320        330        340        350        360 
QHHKDRAEHM MIVDLVRNDL GRVGRFGSVN VQEIVGAENY SVVMHIVSRV TGSLNEAFEA 

       370        380        390        400        410        420 
MEIIRAGFPG GSITGAPKVR AMEIIEELEP QRRDGWGGSI GYIAYRGNIG YRIAIRTLFA 

       430        440        450        460        470 
CNGQLFASSG AGLVGDSMED GEYNETFEKM RALRSFFCAA VHMGKTPYLS 

« Hide

References

[1]"Cloning, nucleotide sequence and expression in Streptomyces lividans and Escherichia coli of pabB from Lactococcus lactis subsp. lactis NCDO 496."
Arhin F.F., Vining L.C.
J. Gen. Microbiol. 139:1785-1793(1993) [PubMed: 8409921] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 11454 / DSM 20729 / NCDO 496 / NCIB 8586.
[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
M64860 Unassigned DNA. Translation: AAA17025.1.

3D structure databases

ProteinModelPortalP27629.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR005801. ADC_synthase.
IPR019999. Anth_synth_I.
IPR006805. Anth_synth_I_N.
IPR015890. Chorismate-bd_C.
IPR010118. Para-NH2Bz/anthranilate_synth.
[Graphical view]
Gene3DG3DSA:3.60.120.10. TRPE_1_chor_bd. 1 hit.
PfamPF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view]
PRINTSPR00095. ANTSNTHASEI.
SUPFAMSSF56322. TRPE_1_chor_bd. 1 hit.
TIGRFAMsTIGR01824. PabB-clade2. 1 hit.
ProtoNetSearch...

Entry information

Entry namePABB_LACLL
AccessionPrimary (citable) accession number: P27629
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 19, 2011
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families