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P77357 (ABGA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
p-aminobenzoyl-glutamate hydrolase subunit A

EC=3.5.1.-
Alternative name(s):
PABA-GLU hydrolase
Short name=PGH
Gene names
Name:abgA
Synonyms:ydaJ
Ordered Locus Names:b1338, JW5205
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p-aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified. Ref.4 Ref.6

Cofactor

Manganese. Ref.4

Subunit structure

Forms a heterodimer with AbgB. Ref.4

Induction

Could be transcriptionally regulated by AbgR. Ref.5

Sequence similarities

Belongs to the peptidase M20 family.

Biophysicochemical properties

Kinetic parameters:

KM=60 µM for PABA-GLU (at pH 8.5) Ref.4

Ontologies

Keywords
   Molecular functionHydrolase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processfolic acid catabolic process

Inferred from genetic interaction Ref.5. Source: EcoliWiki

   Cellular_componentcytoplasm

Inferred from direct assay Ref.4. Source: EcoliWiki

   Molecular_functionpara-aminobenzoyl-glutamate hydrolase activity

Inferred from direct assay Ref.4. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 436436p-aminobenzoyl-glutamate hydrolase subunit A
PRO_0000061958

Sequences

Sequence LengthMass (Da)Tools
P77357 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: CAA22D6925D61F56

FASTA43646,588
        10         20         30         40         50         60 
MESLNQFVNS LAPKLSHWRR DFHHYAESGW VEFRTATLVA EELHQLGYSL ALGREVVNES 

        70         80         90        100        110        120 
SRMGLPDEFT LQREFERARQ QGALAQWIAA FEGGFTGIVA TLDTGRPGPV MAFRVDMDAL 

       130        140        150        160        170        180 
DLSEEQDVSH RPYRDGFASC NAGMMHACGH DGHTAIGLGL AHTLKQFESG LHGVIKLIFQ 

       190        200        210        220        230        240 
PAEEGTRGAR AMVDAGVVDD VDYFTAVHIG TGVPAGTVVC GSDNFMATTK FDAHFTGTAA 

       250        260        270        280        290        300 
HAGAKPEDGH NALLAAAQAT LALHAIAPHS EGASRVNVGV MQAGSGRNVV PASALLKVET 

       310        320        330        340        350        360 
RGASDVINQY VFDRAQQAIQ GAATMYGVGV ETRLMGAATA SSPSPQWVAW LQSQAAQVAG 

       370        380        390        400        410        420 
VNQAIERVEA PAGSEDATLM MARVQQHQGQ ASYVVFGTQL AAGHHNEKFD FDEQVLAIAV 

       430 
ETLARTALNF PWTRGI 

« Hide

References

« Hide 'large scale' references
[1]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"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 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"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.
[4]"Purification and characterization of the folate catabolic enzyme p-aminobenzoyl-glutamate hydrolase from Escherichia coli."
Green J.M., Hollandsworth R., Pitstick L., Carter E.L.
J. Bacteriol. 192:2407-2413(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION AS A PABA-GLU HYDROLASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR.
[5]"Characterization of mutations that allow p-aminobenzoyl-glutamate utilization by Escherichia coli."
Hussein M.J., Green J.M., Nichols B.P.
J. Bacteriol. 180:6260-6268(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[6]"Escherichia coli abg genes enable uptake and cleavage of the folate catabolite p-aminobenzoyl-glutamate."
Carter E.L., Jager L., Gardner L., Hall C.C., Willis S., Green J.M.
J. Bacteriol. 189:3329-3334(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A PABA-GLU HYDROLASE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC74420.2.
AP009048 Genomic DNA. Translation: BAA14940.2.
PIRE64883.
RefSeqNP_415854.4. NC_000913.2.
YP_489608.1. NC_007779.1.

3D structure databases

ProteinModelPortalP77357.
SMRP77357. Positions 4-434.
ModBaseSearch...

Protein-protein interaction databases

STRING511145.b1338.

Protein family/group databases

MEROPSM20.020.

Proteomic databases

PRIDEP77357.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74420; AAC74420; b1338.
BAA14940; BAA14940; BAA14940.
GeneID12932860.
945742.
KEGGecj:Y75_p1315.
eco:b1338.
PATRIC32117952. VBIEscCol129921_1396.

Organism-specific databases

EchoBASEEB3135.
EcoGeneEG13352. abgA.

Phylogenomic databases

eggNOGCOG1473.
HOGENOMHOG000241405.
KOK12940.
OMAYVFERAQ.
ProtClustDBCLSK870441.

Enzyme and pathway databases

BioCycEcoCyc:G6670-MONOMER.
ECOL316407:JW5205-MONOMER.
MetaCyc:G6670-MONOMER.

Gene expression databases

GenevestigatorP77357.

Family and domain databases

InterProIPR017439. Amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFPIRSF005962. Pept_M20D_amidohydro. 1 hit.
SUPFAMSSF55031. Peptidase_M20_dimer. 1 hit.
TIGRFAMsTIGR01891. amidohydrolases. 1 hit.
ProtoNetSearch...

Entry information

Entry nameABGA_ECOLI
AccessionPrimary (citable) accession number: P77357
Secondary accession number(s): P76847
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 11, 2001
Last modified: May 1, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Escherichia coli

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

SIMILARITY comments

Index of protein domains and families