P77357 (ABGA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	436 AA.
Sequence status	Complete.
Protein existence	Evidence 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 function	Hydrolase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	folic acid catabolic process Inferred from genetic interaction Ref.5. Source: EcoliWiki
Cellular_component	cytoplasm Inferred from direct assay Ref.4. Source: EcoliWiki
Molecular_function	para-aminobenzoyl-glutamate hydrolase activity Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 436	436	p-aminobenzoyl-glutamate hydrolase subunit A		PRO_0000061958

Sequences

	Sequence		Length	Mass (Da)
	P77357 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: CAA22D6925D61F56	FASTA	436	46,588
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
PIR	E64883.
RefSeq	NP_415854.4. NC_000913.2. YP_489608.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P77357.
SMR	P77357. Positions 4-434.
ModBase	Search...
Protein-protein interaction databases
STRING	511145.b1338.
Protein family/group databases
MEROPS	M20.020.
Proteomic databases
PRIDE	P77357.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74420; AAC74420; b1338. BAA14940; BAA14940; BAA14940.
GeneID	12932860. 945742.
KEGG	ecj:Y75_p1315. eco:b1338.
PATRIC	32117952. VBIEscCol129921_1396.
Organism-specific databases
EchoBASE	EB3135.
EcoGene	EG13352. abgA.
Phylogenomic databases
eggNOG	COG1473.
HOGENOM	HOG000241405.
KO	K12940.
OMA	YVFERAQ.
ProtClustDB	CLSK870441.
Enzyme and pathway databases
BioCyc	EcoCyc:G6670-MONOMER. ECOL316407:JW5205-MONOMER. MetaCyc:G6670-MONOMER.
Gene expression databases
Genevestigator	P77357.
Family and domain databases
InterPro	IPR017439. Amidohydrolase. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. [Graphical view]
Pfam	PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view]
PIRSF	PIRSF005962. Pept_M20D_amidohydro. 1 hit.
SUPFAM	SSF55031. Peptidase_M20_dimer. 1 hit.
TIGRFAMs	TIGR01891. amidohydrolases. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ABGA_ECOLI

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program