LAAA_PSEFS
ID LAAA_PSEFS Reviewed; 310 AA.
AC C3K630;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=L-amino acid amidase {ECO:0000250|UniProtKB:Q76KX0};
DE EC=3.5.1.101;
GN Name=laaA {ECO:0000250|UniProtKB:Q76KX0}; OrderedLocusNames=PFLU_1629;
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
CC -!- FUNCTION: Hydrolyzes L-prolinamide, L-proline-p-nitroanilide, L-
CC alaninamide, L-methioninamide, piperidine-2-carboxamide and piperazine-
CC 2-carboxamide. Has a much lower activity towards piperazine-2-tert-
CC butylcarboxamide. Does not hydrolyze dipeptides and D-prolinamide.
CC {ECO:0000250|UniProtKB:Q76KX0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-piperazine-2-carboxamide + H2O = (S)-piperazine-2-
CC carboxylate + NH4(+); Xref=Rhea:RHEA:26550, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58919, ChEBI:CHEBI:58920;
CC EC=3.5.1.101; Evidence={ECO:0000250|UniProtKB:Q76KX0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-prolinamide = L-proline + NH4(+);
CC Xref=Rhea:RHEA:26510, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58495, ChEBI:CHEBI:60039; EC=3.5.1.101;
CC Evidence={ECO:0000250|UniProtKB:Q76KX0};
CC -!- ACTIVITY REGULATION: Completely inhibited by ZnSO(4), ZnCl(2), AgNO(3),
CC CdCl(2) and HgCl(2). Partially inhibited by PbCl(2), NiCl(2) and
CC CoCl(2). Unaffected by LiBr, H(2)BO(3), NaCl, MgSO(4), AlCl(3), KCl,
CC CaCl(2), CrCl(3), MnCl(2), FeSO(4), Fe(NH(4))(2)(SO(4))(2), CuSO(4),
CC RbCl, Na(2)MoO(4), (NH(4))(6)Mo(7)O(24), SnCl(2), CsCl and BaCl(2).
CC Completely inhibited by phenylhydrazine, but not by the other carbonyl
CC reagents hydroxylamine, hydrazine, D,L-penicillamine and D-cycloserine.
CC Unaffected by the chelating agents o-phenanthroline, 8-
CC hydroxyquinoline, enthylenediaminetetraacetic acid and alpha,alpha'-
CC dipyridyl. Partially inhibited by the thiol reagents p-
CC chloromercuribenzoate, iodoacetate and N-ethylmaleimide. Not affected
CC by the serine protease inhibitor phenylmethanesulfonyl fluoride, the
CC serine/cysteine protease inhibitor leupeptine or the aspartic protease
CC inhibitor pepstatin. {ECO:0000250|UniProtKB:Q76KX0}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q76KX0}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR EMBL; AM181176; CAY47879.1; -; Genomic_DNA.
DR RefSeq; WP_012722916.1; NC_012660.1.
DR AlphaFoldDB; C3K630; -.
DR SMR; C3K630; -.
DR STRING; 216595.PFLU_1629; -.
DR ESTHER; psefs-laaa; Proline_iminopeptidase.
DR EnsemblBacteria; CAY47879; CAY47879; PFLU_1629.
DR KEGG; pfs:PFLU_1629; -.
DR eggNOG; COG2267; Bacteria.
DR HOGENOM; CLU_020336_15_1_6; -.
DR OMA; TWYRVTG; -.
DR OrthoDB; 1282004at2; -.
DR Proteomes; UP000002332; Chromosome.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR002410; Peptidase_S33.
DR InterPro; IPR005945; Pro_imino_pep.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF005539; Pept_S33_TRI_F1; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01250; pro_imino_pep_2; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..310
FT /note="L-amino acid amidase"
FT /id="PRO_0000400096"
FT DOMAIN 33..284
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 111
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 251
FT /evidence="ECO:0000250"
FT ACT_SITE 278
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 310 AA; 34481 MW; 62753DED28D5AD1B CRC64;
MEFIEKIREG YAAFGAYQTW YRVTGDLSSG RTPLVVIHGG PGCTHDYVDA FKDVAASGHA
VIHYDQLGNG RSTHLPDKDP SFWTVGLFLE ELNNLLDHLQ ISDNYAILGQ SWGGMLGSEH
AILQPKGLRA FIPANSPTCM RTWVSEANRL RKLLPEGVHE TLLKHEAAGT YQDPEYLAAS
RVFYDHHVCR VNPWPEEVAR TFAQVDADPT VYHAMSGPTE FHVIGSLKDW KSIGRLSAIN
VPTLVISGRH DEATPLVVKP FLDEIADVRW ALFEDSSHMP HVEERQACMG TVVKFLDEVC
SVPHNVLKAG
