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P28305

- PABC_ECOLI

UniProt

P28305 - PABC_ECOLI

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Protein

Aminodeoxychorismate lyase

Gene

pabC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of p-aminobenzoate (PABA), a precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate.2 Publications

Catalytic activityi

4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate.1 Publication

Cofactori

Pyridoxal phosphate.3 Publications

Pathwayi

GO - Molecular functioni

  1. 4-amino-4-deoxychorismate lyase activity Source: UniProtKB
  2. pyridoxal phosphate binding Source: EcoCyc

GO - Biological processi

  1. folic acid biosynthetic process Source: UniProtKB-KW
  2. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Folate biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:ADCLY-MONOMER.
ECOL316407:JW1082-MONOMER.
MetaCyc:ADCLY-MONOMER.
BRENDAi4.1.3.38. 2026.
UniPathwayiUPA00077; UER00150.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminodeoxychorismate lyase (EC:4.1.3.38)
Alternative name(s):
4-amino-4-deoxychorismate lyase
Short name:
ADC lyase
Short name:
ADCL
Gene namesi
Name:pabC
Ordered Locus Names:b1096, JW1082
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11493. pabC.

Pathology & Biotechi

Disruption phenotypei

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 269269Aminodeoxychorismate lyasePRO_0000103305Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei140 – 1401N6-(pyridoxal phosphate)lysine

Proteomic databases

PRIDEiP28305.

Expressioni

Gene expression databases

GenevestigatoriP28305.

Interactioni

Subunit structurei

Homodimer.4 Publications

Protein-protein interaction databases

DIPiDIP-10435N.
IntActiP28305. 8 interactions.
STRINGi511145.b1096.

Structurei

Secondary structure

1
269
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43
Beta strandi7 – 104
Helixi17 – 215
Beta strandi24 – 329
Helixi39 – 5214
Helixi60 – 7415
Beta strandi76 – 849
Beta strandi101 – 1077
Helixi112 – 1198
Beta strandi121 – 1255
Turni134 – 1374
Helixi145 – 15410
Turni155 – 1584
Beta strandi160 – 1667
Beta strandi169 – 1735
Beta strandi175 – 1839
Beta strandi186 – 1905
Beta strandi193 – 1975
Helixi200 – 21112
Beta strandi212 – 2198
Helixi223 – 2275
Beta strandi230 – 2356
Beta strandi237 – 2393
Beta strandi241 – 2477
Helixi256 – 26611

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ET0X-ray2.20A1-269[»]
1I2KX-ray1.79A1-269[»]
1I2LX-ray2.30A1-269[»]
ProteinModelPortaliP28305.
SMRiP28305. Positions 1-269.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28305.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0115.
HOGENOMiHOG000276707.
InParanoidiP28305.
KOiK02619.
OMAiIEGVYSN.
OrthoDBiEOG67MF3R.
PhylomeDBiP28305.

Family and domain databases

InterProiIPR017824. Aminodeoxychorismate_lyase_IV.
IPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
[Graphical view]
PANTHERiPTHR11825. PTHR11825. 1 hit.
PfamiPF01063. Aminotran_4. 1 hit.
[Graphical view]
SUPFAMiSSF56752. SSF56752. 1 hit.
TIGRFAMsiTIGR03461. pabC_Proteo. 1 hit.
PROSITEiPS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28305-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFLINGHKQE SLAVSDRATQ FGDGCFTTAR VIDGKVSLLS AHIQRLQDAC
60 70 80 90 100
QRLMISCDFW PQLEQEMKTL AAEQQNGVLK VVISRGSGGR GYSTLNSGPA
110 120 130 140 150
TRILSVTAYP AHYDRLRNEG ITLALSPVRL GRNPHLAGIK HLNRLEQVLI
160 170 180 190 200
RSHLEQTNAD EALVLDSEGW VTECCAANLF WRKGNVVYTP RLDQAGVNGI
210 220 230 240 250
MRQFCIRLLA QSSYQLVEVQ ASLEESLQAD EMVICNALMP VMPVCACGDV
260
SFSSATLYEY LAPLCERPN
Length:269
Mass (Da):29,715
Last modified:December 1, 1992 - v1
Checksum:i4BC186083F5E999E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M93135 Genomic DNA. Translation: AAA24267.1.
U00096 Genomic DNA. Translation: AAC74180.1.
AP009048 Genomic DNA. Translation: BAA35904.1.
PIRiA42954.
RefSeqiNP_415614.1. NC_000913.3.
YP_489364.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74180; AAC74180; b1096.
BAA35904; BAA35904; BAA35904.
GeneIDi12930426.
946647.
KEGGiecj:Y75_p1066.
eco:b1096.
PATRICi32117433. VBIEscCol129921_1139.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M93135 Genomic DNA. Translation: AAA24267.1 .
U00096 Genomic DNA. Translation: AAC74180.1 .
AP009048 Genomic DNA. Translation: BAA35904.1 .
PIRi A42954.
RefSeqi NP_415614.1. NC_000913.3.
YP_489364.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ET0 X-ray 2.20 A 1-269 [» ]
1I2K X-ray 1.79 A 1-269 [» ]
1I2L X-ray 2.30 A 1-269 [» ]
ProteinModelPortali P28305.
SMRi P28305. Positions 1-269.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10435N.
IntActi P28305. 8 interactions.
STRINGi 511145.b1096.

Chemistry

BindingDBi P28305.
ChEMBLi CHEMBL1075099.

Proteomic databases

PRIDEi P28305.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74180 ; AAC74180 ; b1096 .
BAA35904 ; BAA35904 ; BAA35904 .
GeneIDi 12930426.
946647.
KEGGi ecj:Y75_p1066.
eco:b1096.
PATRICi 32117433. VBIEscCol129921_1139.

Organism-specific databases

EchoBASEi EB1456.
EcoGenei EG11493. pabC.

Phylogenomic databases

eggNOGi COG0115.
HOGENOMi HOG000276707.
InParanoidi P28305.
KOi K02619.
OMAi IEGVYSN.
OrthoDBi EOG67MF3R.
PhylomeDBi P28305.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00150 .
BioCyci EcoCyc:ADCLY-MONOMER.
ECOL316407:JW1082-MONOMER.
MetaCyc:ADCLY-MONOMER.
BRENDAi 4.1.3.38. 2026.

Miscellaneous databases

EvolutionaryTracei P28305.
PROi P28305.

Gene expression databases

Genevestigatori P28305.

Family and domain databases

InterProi IPR017824. Aminodeoxychorismate_lyase_IV.
IPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
[Graphical view ]
PANTHERi PTHR11825. PTHR11825. 1 hit.
Pfami PF01063. Aminotran_4. 1 hit.
[Graphical view ]
SUPFAMi SSF56752. SSF56752. 1 hit.
TIGRFAMsi TIGR03461. pabC_Proteo. 1 hit.
PROSITEi PS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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.

Entry informationi

Entry nameiPABC_ECOLI
AccessioniPrimary (citable) accession number: P28305
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: October 29, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3