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Protein

Aminodeoxychorismate lyase

Gene

pabC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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 5'-phosphate3 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 Componenti: Chromosome UP000000625 Componenti: 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 – 43Combined sources
Beta strandi7 – 104Combined sources
Helixi17 – 215Combined sources
Beta strandi24 – 329Combined sources
Helixi39 – 5214Combined sources
Helixi60 – 7415Combined sources
Beta strandi76 – 849Combined sources
Beta strandi101 – 1077Combined sources
Helixi112 – 1198Combined sources
Beta strandi121 – 1255Combined sources
Turni134 – 1374Combined sources
Helixi145 – 15410Combined sources
Turni155 – 1584Combined sources
Beta strandi160 – 1667Combined sources
Beta strandi169 – 1735Combined sources
Beta strandi175 – 1839Combined sources
Beta strandi186 – 1905Combined sources
Beta strandi193 – 1975Combined sources
Helixi200 – 21112Combined sources
Beta strandi212 – 2198Combined sources
Helixi223 – 2275Combined sources
Beta strandi230 – 2356Combined sources
Beta strandi237 – 2393Combined sources
Beta strandi241 – 2477Combined sources
Helixi256 – 26611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiDEVFVCN.
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

BindingDBiP28305.
ChEMBLiCHEMBL1075099.

Proteomic databases

PRIDEiP28305.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB1456.
EcoGeneiEG11493. pabC.

Phylogenomic databases

eggNOGiCOG0115.
HOGENOMiHOG000276707.
InParanoidiP28305.
KOiK02619.
OMAiDEVFVCN.
OrthoDBiEOG67MF3R.
PhylomeDBiP28305.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP28305.
PROiP28305.

Gene expression databases

GenevestigatoriP28305.

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]
ProtoNetiSearch...

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: March 4, 2015
This is version 125 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.