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P28305 (PABC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Aminodeoxychorismate lyase

EC=4.1.3.38
Alternative name(s):
4-amino-4-deoxychorismate lyase
Short name=ADC lyase
Short name=ADCL
Gene names
Name:pabC
Ordered Locus Names:b1096, JW1082
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length269 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the biosynthesis of p-aminobenzoate (PABA), a precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate. Ref.1 Ref.6

Catalytic activity

4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate. Ref.6

Cofactor

Pyridoxal phosphate. Ref.1 Ref.7 Ref.8

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-aminobenzoate from chorismate: step 2/2.

Subunit structure

Homodimer. Ref.1 Ref.6 Ref.7 Ref.8

Disruption phenotype

Cells lacking this gene are unable to produce PABA. Ref.1

Sequence similarities

Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 269269Aminodeoxychorismate lyase
PRO_0000103305

Amino acid modifications

Modified residue1401N6-(pyridoxal phosphate)lysine

Secondary structure

................................................. 269
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P28305 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 4BC186083F5E999E

FASTA26929,715
        10         20         30         40         50         60 
MFLINGHKQE SLAVSDRATQ FGDGCFTTAR VIDGKVSLLS AHIQRLQDAC QRLMISCDFW 

        70         80         90        100        110        120 
PQLEQEMKTL AAEQQNGVLK VVISRGSGGR GYSTLNSGPA TRILSVTAYP AHYDRLRNEG 

       130        140        150        160        170        180 
ITLALSPVRL GRNPHLAGIK HLNRLEQVLI RSHLEQTNAD EALVLDSEGW VTECCAANLF 

       190        200        210        220        230        240 
WRKGNVVYTP RLDQAGVNGI MRQFCIRLLA QSSYQLVEVQ ASLEESLQAD EMVICNALMP 

       250        260 
VMPVCACGDV SFSSATLYEY LAPLCERPN 

« Hide

References

« Hide 'large scale' references
[1]"Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme."
Green J.M., Merkel W.K., Nichols B.P.
J. Bacteriol. 174:5317-5323(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, COFACTOR.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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 277:1453-1462(1997) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"p-aminobenzoate biosynthesis in Escherichia coli. Purification of aminodeoxychorismate lyase and cloning of pabC."
Green J.M., Nichols B.P.
J. Biol. Chem. 266:12971-12975(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-21.
[6]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
[7]"Three-dimensional structure of 4-amino-4-deoxychorismate lyase from Escherichia coli."
Nakai T., Mizutani H., Miyahara I., Hirotsu K., Takeda S., Jhee K.-H., Yoshimura T., Esaki N.
J. Biochem. 128:29-38(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, COFACTOR, SUBUNIT.
[8]"Structure of Escherichia coli aminodeoxychorismate synthase: architectural conservation and diversity in chorismate-utilizing enzymes."
Parsons J.F., Jensen P.Y., Pachikara A.S., Howard A.J., Eisenstein E., Ladner J.E.
Biochemistry 41:2198-2208(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, COFACTOR, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M93135 Genomic DNA. Translation: AAA24267.1.
U00096 Genomic DNA. Translation: AAC74180.1.
AP009048 Genomic DNA. Translation: BAA35904.1.
PIRA42954.
RefSeqNP_415614.1. NC_000913.3.
YP_489364.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ET0X-ray2.20A1-269[»]
1I2KX-ray1.79A1-269[»]
1I2LX-ray2.30A1-269[»]
ProteinModelPortalP28305.
SMRP28305. Positions 1-269.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10435N.
IntActP28305. 8 interactions.
STRING511145.b1096.

Chemistry

BindingDBP28305.
ChEMBLCHEMBL1075099.

Proteomic databases

PRIDEP28305.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74180; AAC74180; b1096.
BAA35904; BAA35904; BAA35904.
GeneID12930426.
946647.
KEGGecj:Y75_p1066.
eco:b1096.
PATRIC32117433. VBIEscCol129921_1139.

Organism-specific databases

EchoBASEEB1456.
EcoGeneEG11493. pabC.

Phylogenomic databases

eggNOGCOG0115.
HOGENOMHOG000276707.
KOK02619.
OMAIEGVYSN.
OrthoDBEOG67MF3R.
PhylomeDBP28305.

Enzyme and pathway databases

BioCycEcoCyc:ADCLY-MONOMER.
ECOL316407:JW1082-MONOMER.
MetaCyc:ADCLY-MONOMER.
BRENDA4.1.3.38. 2026.
UniPathwayUPA00077; UER00150.

Gene expression databases

GenevestigatorP28305.

Family and domain databases

InterProIPR017824. Aminodeoxychorismate_lyase_IV.
IPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
[Graphical view]
PANTHERPTHR11825. PTHR11825. 1 hit.
PfamPF01063. Aminotran_4. 1 hit.
[Graphical view]
SUPFAMSSF56752. SSF56752. 1 hit.
TIGRFAMsTIGR03461. pabC_Proteo. 1 hit.
PROSITEPS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP28305.
PROP28305.

Entry information

Entry namePABC_ECOLI
AccessionPrimary (citable) accession number: P28305
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: July 9, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene