ID   ABGA_ECOLI              Reviewed;         436 AA.
AC   P77357; P76847;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   02-SEP-2026, entry version 162.
DE   RecName: Full=p-aminobenzoyl-glutamate hydrolase subunit A;
DE            EC=3.5.1.-;
DE   AltName: Full=PABA-GLU hydrolase;
DE            Short=PGH;
GN   Name=abgA; Synonyms=ydaJ; OrderedLocusNames=b1338, JW5205;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-10, FUNCTION AS A PABA-GLU HYDROLASE,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND COFACTOR.
RX   PubMed=20190044; DOI=10.1128/jb.01362-09;
RA   Green J.M., Hollandsworth R., Pitstick L., Carter E.L.;
RT   "Purification and characterization of the folate catabolic enzyme p-
RT   aminobenzoyl-glutamate hydrolase from Escherichia coli.";
RL   J. Bacteriol. 192:2407-2413(2010).
RN   [5]
RP   INDUCTION.
RX   PubMed=9829935; DOI=10.1128/jb.180.23.6260-6268.1998;
RA   Hussein M.J., Green J.M., Nichols B.P.;
RT   "Characterization of mutations that allow p-aminobenzoyl-glutamate
RT   utilization by Escherichia coli.";
RL   J. Bacteriol. 180:6260-6268(1998).
RN   [6]
RP   FUNCTION AS A PABA-GLU HYDROLASE.
RX   PubMed=17307853; DOI=10.1128/jb.01940-06;
RA   Carter E.L., Jager L., Gardner L., Hall C.C., Willis S., Green J.M.;
RT   "Escherichia coli abg genes enable uptake and cleavage of the folate
RT   catabolite p-aminobenzoyl-glutamate.";
RL   J. Bacteriol. 189:3329-3334(2007).
CC   -!- FUNCTION: Component of the p-aminobenzoyl-glutamate hydrolase
CC       multicomponent enzyme system which catalyzes the cleavage of p-
CC       aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and
CC       glutamate. AbgAB does not degrade dipeptides and the physiological role
CC       of abgABT should be clarified. {ECO:0000269|PubMed:17307853,
CC       ECO:0000269|PubMed:20190044}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:20190044};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=60 uM for PABA-GLU (at pH 8.5) {ECO:0000269|PubMed:20190044};
CC   -!- SUBUNIT: Forms a heterodimer with AbgB. {ECO:0000269|PubMed:20190044}.
CC   -!- INTERACTION:
CC       P77357; P76052: abgB; NbExp=2; IntAct=EBI-9155452, EBI-1123629;
CC   -!- INDUCTION: Could be transcriptionally regulated by AbgR.
CC       {ECO:0000269|PubMed:9829935}.
CC   -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR   EMBL; U00096; AAC74420.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA14940.2; -; Genomic_DNA.
DR   PIR; E64883; E64883.
DR   RefSeq; NP_415854.4; NC_000913.3.
DR   RefSeq; WP_000444929.1; NZ_CP009789.1.
DR   AlphaFoldDB; P77357; -.
DR   SMR; P77357; -.
DR   BioGRID; 4261854; 28.
DR   BioGRID; 850109; 1.
DR   ComplexPortal; CPX-28; p-aminobenzoyl-glutamate hydrolase complex.
DR   FunCoup; P77357; 537.
DR   IntAct; P77357; 2.
DR   STRING; 511145.b1338; -.
DR   MEROPS; M20.020; -.
DR   PaxDb; 511145-b1338; -.
DR   EnsemblBacteria; AAC74420; AAC74420; b1338.
DR   GeneID; 945742; -.
DR   KEGG; ecj:JW5205; -.
DR   KEGG; eco:b1338; -.
DR   KEGG; ecoc:C3026_07835; -.
DR   PATRIC; fig|1411691.4.peg.939; -.
DR   EchoBASE; EB3135; -.
DR   eggNOG; COG1473; Bacteria.
DR   HOGENOM; CLU_023257_2_1_6; -.
DR   InParanoid; P77357; -.
DR   OMA; YVFERAQ; -.
DR   OrthoDB; 9777385at2; -.
DR   PhylomeDB; P77357; -.
DR   BioCyc; EcoCyc:G6670-MONOMER; -.
DR   BioCyc; MetaCyc:G6670-MONOMER; -.
DR   SABIO-RK; P77357; -.
DR   PRO; PR:P77357; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:1902494; C:catalytic complex; IPI:ComplexPortal.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0016805; F:dipeptidase activity; IBA:GO_Central.
DR   GO; GO:0071713; F:para-aminobenzoyl-glutamate hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:EcoliWiki.
DR   GO; GO:0046657; P:folic acid catabolic process; IDA:ComplexPortal.
DR   CDD; cd05665; M20_Acy1_IAAspH; 1.
DR   FunFam; 3.40.630.10:FF:000080; p-aminobenzoyl-glutamate hydrolase subunit A; 1.
DR   FunFam; 3.40.630.10:FF:000077; p-aminobenzoyl-glutamate hydrolase, A subunit; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR033845; AbgA.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR052030; Peptidase_M20/M20A_hydrolases.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR30575; PEPTIDASE M20; 1.
DR   PANTHER; PTHR30575:SF3; PEPTIDASE M20 DIMERISATION DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Reference proteome.
FT   CHAIN           1..436
FT                   /note="p-aminobenzoyl-glutamate hydrolase subunit A"
FT                   /id="PRO_0000061958"
SQ   SEQUENCE   436 AA;  46588 MW;  CAA22D6925D61F56 CRC64;
     MESLNQFVNS LAPKLSHWRR DFHHYAESGW VEFRTATLVA EELHQLGYSL ALGREVVNES
     SRMGLPDEFT LQREFERARQ QGALAQWIAA FEGGFTGIVA TLDTGRPGPV MAFRVDMDAL
     DLSEEQDVSH RPYRDGFASC NAGMMHACGH DGHTAIGLGL AHTLKQFESG LHGVIKLIFQ
     PAEEGTRGAR AMVDAGVVDD VDYFTAVHIG TGVPAGTVVC GSDNFMATTK FDAHFTGTAA
     HAGAKPEDGH NALLAAAQAT LALHAIAPHS EGASRVNVGV MQAGSGRNVV PASALLKVET
     RGASDVINQY VFDRAQQAIQ GAATMYGVGV ETRLMGAATA SSPSPQWVAW LQSQAAQVAG
     VNQAIERVEA PAGSEDATLM MARVQQHQGQ ASYVVFGTQL AAGHHNEKFD FDEQVLAIAV
     ETLARTALNF PWTRGI
//