ID   ABGA_HAEIN              Reviewed;         423 AA.
AC   P44765;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=p-aminobenzoyl-glutamate hydrolase subunit A homolog;
DE            EC=3.5.1.-;
DE   AltName: Full=PABA-GLU hydrolase;
DE            Short=PGH;
GN   Name=abgA; OrderedLocusNames=HI_0584;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Catalyzes the cleavage of p-aminobenzoyl-glutamate (PABA-GLU)
CC       to form p-aminobenzoate (PABA) and glutamate. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- MISCELLANEOUS: Unlike E.coli, AbgB is not present in H.influenza and
CC       therefore the multicomponent hydrolase AbgAB does not exist in this
CC       form.
CC   -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR   EMBL; L42023; AAC22243.1; -; Genomic_DNA.
DR   PIR; B64079; B64079.
DR   RefSeq; NP_438742.1; NC_000907.1.
DR   RefSeq; WP_005694556.1; NC_000907.1.
DR   AlphaFoldDB; P44765; -.
DR   SMR; P44765; -.
DR   STRING; 71421.HI_0584; -.
DR   EnsemblBacteria; AAC22243; AAC22243; HI_0584.
DR   KEGG; hin:HI_0584; -.
DR   PATRIC; fig|71421.8.peg.605; -.
DR   eggNOG; COG1473; Bacteria.
DR   HOGENOM; CLU_023257_2_1_6; -.
DR   OMA; HHEAEFD; -.
DR   PhylomeDB; P44765; -.
DR   BioCyc; HINF71421:G1GJ1-597-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016805; F:dipeptidase activity; IBA:GO_Central.
DR   GO; GO:0071713; F:para-aminobenzoyl-glutamate hydrolase activity; IBA:GO_Central.
DR   GO; GO:0046657; P:folic acid catabolic process; IBA:GO_Central.
DR   CDD; cd05665; M20_Acy1_IAAspH; 1.
DR   InterPro; IPR033845; AbgA.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01891; amidohydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..423
FT                   /note="p-aminobenzoyl-glutamate hydrolase subunit A
FT                   homolog"
FT                   /id="PRO_0000061959"
SQ   SEQUENCE   423 AA;  46554 MW;  E5887A9FBAD15DD7 CRC64;
     MNLDLNQLVK WHREFHRFPE IGWSEFWTTS RIADYLEDLD CFEIFLGKQI INPDFVRGRK
     QAVVDKGLAN AKAYGANEKW LEKMEGYTGC VALFDSGKPG KTIALRFDID CVNVTETRSP
     EHIPNKEGFA SINDGFMHAC GHDSHITIGL GVALWIAQNK DKLTGKVKIV FQPAEEGVRG
     AAAIAQSGII DDADYFASSH ISFCANTGTV IANPRNFLST TKIDIRYKGK PAHAGAAPHL
     GRNALLAAAH TVTQLHGIAR HGKGMTRINV GVLKAGEGRN VIPSSAELQL EVRGENKAIN
     EYMTEQVMQI AKGISISFNV AYETEIVGEA VDMNNDVELI KLIEEISLEQ PQINNVNSDY
     AFNASEDATI LGRRVQEHGG KAIYFILGAD RTAGHHEAEF DFDENQLLTG VNIYTSLVQK
     LLS