AMIE_PSEAE
ID AMIE_PSEAE Reviewed; 346 AA.
AC P11436;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Aliphatic amidase;
DE EC=3.5.1.4;
DE AltName: Full=Acylamide amidohydrolase;
GN Name=amiE; OrderedLocusNames=PA3366;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=PAC142;
RX PubMed=3108029; DOI=10.1016/0014-5793(87)80163-1;
RA Ambler R.P., Auffret A.D., Clarke P.H.;
RT "The amino acid sequence of the aliphatic amidase from Pseudomonas
RT aeruginosa.";
RL FEBS Lett. 215:285-290(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3108030; DOI=10.1016/0014-5793(87)80164-3;
RA Brammar W.J., Charles I.G., Matfield M., Liu C.-P., Drew R.E., Clarke P.H.;
RT "The nucleotide sequence of the amiE gene of Pseudomonas aeruginosa.";
RL FEBS Lett. 215:291-294(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 336-346.
RX PubMed=7539417; DOI=10.1128/jb.177.11.3052-3057.1995;
RA Wilson S.A., Drew R.E.;
RT "Transcriptional analysis of the amidase operon from Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 177:3052-3057(1995).
RN [5]
RP SUBUNIT, AND MUTAGENESIS OF CYS-166.
RX PubMed=10359655; DOI=10.1042/bj3400711;
RA Farnaud S., Tata R., Sohi M.K., Wan T., Brown P.R., Sutton B.J.;
RT "Evidence that cysteine-166 is the active-site nucleophile of Pseudomonas
RT aeruginosa amidase: crystallization and preliminary X-ray diffraction
RT analysis of the enzyme.";
RL Biochem. J. 340:711-714(1999).
RN [6]
RP MUTAGENESIS OF GLU-59 AND LYS-134, AND 3D-STRUCTURE MODELING OF 20-290.
RX PubMed=11955282; DOI=10.1042/bj20011714;
RA Novo C., Farnaud S., Tata R., Clemente A., Brown P.R.;
RT "Support for a three-dimensional structure predicting a Cys-Glu-Lys
RT catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed
RT mutagenesis and mutations altering substrate specificity.";
RL Biochem. J. 365:731-738(2002).
CC -!- FUNCTION: Catalyzes the hydrolysis of short-chain aliphatic amides to
CC their corresponding organic acids with release of ammonia. Enables the
CC organism to use acetamide as both carbon and nitrogen source.
CC -!- FUNCTION: Also exhibits in vitro acyl transferase activity,
CC transferring the acyl moiety of short-chain amides to hydroxylamine to
CC form hydroxamates. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate +
CC NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4;
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:10359655}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Aliphatic amidase family. {ECO:0000305}.
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DR EMBL; M27612; AAA25697.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06754.1; -; Genomic_DNA.
DR PIR; A26741; A26741.
DR PIR; H83222; H83222.
DR RefSeq; NP_252056.1; NC_002516.2.
DR RefSeq; WP_003113129.1; NZ_QZGE01000017.1.
DR PDB; 2UXY; X-ray; 1.25 A; A=1-341.
DR PDBsum; 2UXY; -.
DR AlphaFoldDB; P11436; -.
DR SMR; P11436; -.
DR STRING; 287.DR97_4561; -.
DR PaxDb; P11436; -.
DR DNASU; 877816; -.
DR EnsemblBacteria; AAG06754; AAG06754; PA3366.
DR GeneID; 877816; -.
DR KEGG; pae:PA3366; -.
DR PATRIC; fig|208964.12.peg.3525; -.
DR PseudoCAP; PA3366; -.
DR HOGENOM; CLU_071797_0_0_6; -.
DR InParanoid; P11436; -.
DR OMA; PWVPIEG; -.
DR PhylomeDB; P11436; -.
DR BioCyc; PAER208964:G1FZ6-3430-MON; -.
DR BRENDA; 3.5.1.4; 5087.
DR SABIO-RK; P11436; -.
DR EvolutionaryTrace; P11436; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0004040; F:amidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0015976; P:carbon utilization; IDA:PseudoCAP.
DR GO; GO:0043605; P:cellular amide catabolic process; IDA:PseudoCAP.
DR Gene3D; 3.60.110.10; -; 1.
DR HAMAP; MF_01242; Aliphatic_amidase; 1.
DR InterPro; IPR023719; Aliphatic_amidase.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Reference proteome.
FT CHAIN 1..346
FT /note="Aliphatic amidase"
FT /id="PRO_0000204060"
FT DOMAIN 13..260
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 59
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 134
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 166
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT MUTAGEN 59
FT /note="E->Q,D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11955282"
FT MUTAGEN 134
FT /note="K->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11955282"
FT MUTAGEN 134
FT /note="K->R: 200-fold reduction in activity."
FT /evidence="ECO:0000269|PubMed:11955282"
FT MUTAGEN 166
FT /note="C->S,A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10359655"
FT CONFLICT 40
FT /note="E -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="G -> P (in Ref. 2; AAA25697)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="E -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:2UXY"
FT HELIX 28..48
FT /evidence="ECO:0007829|PDB:2UXY"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:2UXY"
FT TURN 59..63
FT /evidence="ECO:0007829|PDB:2UXY"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:2UXY"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2UXY"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:2UXY"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:2UXY"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:2UXY"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:2UXY"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:2UXY"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:2UXY"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:2UXY"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:2UXY"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:2UXY"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:2UXY"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:2UXY"
FT HELIX 197..211
FT /evidence="ECO:0007829|PDB:2UXY"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:2UXY"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:2UXY"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:2UXY"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2UXY"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:2UXY"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:2UXY"
FT HELIX 260..269
FT /evidence="ECO:0007829|PDB:2UXY"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:2UXY"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:2UXY"
FT HELIX 303..310
FT /evidence="ECO:0007829|PDB:2UXY"
FT HELIX 312..322
FT /evidence="ECO:0007829|PDB:2UXY"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:2UXY"
SQ SEQUENCE 346 AA; 38495 MW; E19CEB474EB92B93 CRC64;
MRHGDISSSN DTVGVAVVNY KMPRLHTAAE VLDNARKIAE MIVGMKQGLP GMDLVVFPEY
SLQGIMYDPA EMMETAVAIP GEETEIFSRA CRKANVWGVF SLTGERHEEH PRKAPYNTLV
LIDNNGEIVQ KYRKIIPWCP IEGWYPGGQT YVSEGPKGMK ISLIICDDGN YPEIWRDCAM
KGAELIVRCQ GYMYPAKDQQ VMMAKAMAWA NNCYVAVANA AGFDGVYSYF GHSAIIGFDG
RTLGECGEEE MGIQYAQLSL SQIRDARAND QSQNHLFKIL HRGYSGLQAS GDGDRGLAEC
PFEFYRTWVT DAEKARENVE RLTRSTTGVA QCPVGRLPYE GLEKEA
