ABGB_ECOLI
ID ABGB_ECOLI Reviewed; 481 AA.
AC P76052; Q2MBF2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=p-aminobenzoyl-glutamate hydrolase subunit B;
DE EC=3.5.1.-;
DE AltName: Full=PABA-GLU hydrolase;
DE Short=PGH;
GN Name=abgB; Synonyms=ydaI; OrderedLocusNames=b1337, JW1331;
GN ORFNames=ECK1333;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
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 [4]
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 [5]
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 AbgA. {ECO:0000269|PubMed:20190044}.
CC -!- INTERACTION:
CC P76052; P77357: abgA; NbExp=2; IntAct=EBI-1123629, EBI-9155452;
CC -!- INDUCTION: Could be transcriptionally regulated by AbgR.
CC {ECO:0000269|PubMed:9829935}.
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DR EMBL; U00096; AAC74419.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76404.1; -; Genomic_DNA.
DR PIR; D64883; D64883.
DR RefSeq; NP_415853.1; NC_000913.3.
DR RefSeq; WP_001156451.1; NZ_SSZK01000012.1.
DR AlphaFoldDB; P76052; -.
DR SMR; P76052; -.
DR BioGRID; 4260157; 64.
DR ComplexPortal; CPX-28; p-aminobenzoyl-glutamate hydrolase complex.
DR IntAct; P76052; 6.
DR STRING; 511145.b1337; -.
DR PaxDb; P76052; -.
DR PRIDE; P76052; -.
DR EnsemblBacteria; AAC74419; AAC74419; b1337.
DR EnsemblBacteria; BAE76404; BAE76404; BAE76404.
DR GeneID; 945950; -.
DR KEGG; ecj:JW1331; -.
DR KEGG; eco:b1337; -.
DR PATRIC; fig|1411691.4.peg.940; -.
DR EchoBASE; EB3134; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_031812_0_1_6; -.
DR InParanoid; P76052; -.
DR OMA; HYAITDT; -.
DR PhylomeDB; P76052; -.
DR BioCyc; EcoCyc:G6669-MON; -.
DR BioCyc; MetaCyc:G6669-MON; -.
DR PRO; PR:P76052; -.
DR Proteomes; UP000000318; Chromosome.
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 InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR017145; Aminobenzoyl-glu_utiliz_pB.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037227; Aminobenzoyl-glu_utiliz_pB; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01891; amidohydrolases; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Reference proteome.
FT CHAIN 1..481
FT /note="p-aminobenzoyl-glutamate hydrolase subunit B"
FT /id="PRO_0000064421"
SQ SEQUENCE 481 AA; 52194 MW; 84B09100A563E07C CRC64;
MQEIYRFIDD AIEADRQRYT DIADQIWDHP ETRFEEFWSA EHLASALESA GFTVTRNVGN
IPNAFIASFG QGKPVIALLG EYDALAGLSQ QAGCAQPTSV TPGENGHGCG HNLLGTAAFA
AAIAVKKWLE QYGQGGTVRF YGCPGEEGGS GKTFMVREGV FDDVDAALTW HPEAFAGMFN
TRTLANIQAS WRFKGIAAHA ANSPHLGRSA LDAVTLMTTG TNFLNEHIIE KARVHYAITN
SGGISPNVVQ AQAEVLYLIR APEMTDVQHI YDRVAKIAEG AALMTETTVE CRFDKACSSY
LPNRTLENAM YQALSHFGTP EWNSEELAFA KQIQATLTSN DRQNSLNNIA ATGGENGKVF
ALRHRETVLA NEVAPYAATD NVLAASTDVG DVSWKLPVAQ CFSPCFAVGT PLHTWQLVSQ
GRTSIAHKGM LLAAKTMAAT TVNLFLDSGL LQECQQEHQQ VTDTQPYHCP IPKNVTPSPL
K
