AMIE_BACSP
ID AMIE_BACSP Reviewed; 348 AA.
AC Q9L543;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Aliphatic amidase;
DE EC=3.5.1.4;
DE AltName: Full=Acylamide amidohydrolase;
GN Name=amiE; Synonyms=ami;
OS Bacillus sp.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1409;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=BR499;
RX PubMed=10978771; DOI=10.1016/s0141-0229(00)00248-9;
RA Kim S.-H., Oriel P.J.;
RT "Cloning and expression of the nitrile hydratase and amidase genes from
RT Bacillus sp. BR449 into Escherichia coli.";
RL Enzyme Microb. Technol. 27:492-501(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RAPc8;
RA Cameron R.A., Cowan D.A.;
RT "Cloning, expression and characterization of the nitrile hydratase and
RT amidase of a moderately thermophilic Bacillus sp.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolysis of short-chain aliphatic amides to
CC their corresponding organic acids with release of ammonia.
CC {ECO:0000269|PubMed:10978771}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable up to at least 50 degrees Celsius.;
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Aliphatic amidase family. {ECO:0000305}.
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DR EMBL; AF257487; AAF69000.1; -; Genomic_DNA.
DR EMBL; AY184492; AAO23013.1; -; Genomic_DNA.
DR PDB; 2PLQ; X-ray; 1.90 A; A=1-348.
DR PDB; 4GYL; X-ray; 1.90 A; A=1-348.
DR PDB; 4GYN; X-ray; 1.90 A; A=1-348.
DR PDB; 4KZF; X-ray; 1.85 A; A=1-348.
DR PDB; 4LF0; X-ray; 1.10 A; A=1-348.
DR PDBsum; 2PLQ; -.
DR PDBsum; 4GYL; -.
DR PDBsum; 4GYN; -.
DR PDBsum; 4KZF; -.
DR PDBsum; 4LF0; -.
DR AlphaFoldDB; Q9L543; -.
DR SMR; Q9L543; -.
DR EvolutionaryTrace; Q9L543; -.
DR GO; GO:0004040; F:amidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
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; Hydrolase.
FT CHAIN 1..348
FT /note="Aliphatic amidase"
FT /id="PRO_0000204055"
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 STRAND 12..18
FT /evidence="ECO:0007829|PDB:4LF0"
FT HELIX 28..48
FT /evidence="ECO:0007829|PDB:4LF0"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:4LF0"
FT TURN 59..63
FT /evidence="ECO:0007829|PDB:4LF0"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:4LF0"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4LF0"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:4LF0"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:4LF0"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:4LF0"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:4LF0"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:4LF0"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:4LF0"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:4LF0"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:4LF0"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:4LF0"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:4LF0"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:4LF0"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:4KZF"
FT HELIX 197..211
FT /evidence="ECO:0007829|PDB:4LF0"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:4LF0"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:4LF0"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:4LF0"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:4LF0"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:4LF0"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:4LF0"
FT HELIX 260..269
FT /evidence="ECO:0007829|PDB:4LF0"
FT HELIX 275..279
FT /evidence="ECO:0007829|PDB:4LF0"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:4LF0"
FT HELIX 303..310
FT /evidence="ECO:0007829|PDB:4LF0"
FT HELIX 312..322
FT /evidence="ECO:0007829|PDB:4LF0"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:4LF0"
SQ SEQUENCE 348 AA; 38597 MW; 547B1CBE30AC5FBC CRC64;
MRHGDISSSH DTVGIAVVNY KMPRLHTKAE VIENAKKIAD MVVGMKQGLP GMDLVVFPEY
STMGIMYDQD EMFATAASIP GEETAIFAEA CKKADTWGVF SLTGEKHEDH PNKAPYNTLV
LINNKGEIVQ KYRKIIPWCP IEGWYPGDTT YVTEGPKGLK ISLIVCDDGN YPEIWRDCAM
KGAELIVRCQ GYMYPAKEQQ IMMAKAMAWA NNTYVAVANA TGFDGVYSYF GHSAIIGFDG
RTLGECGTEE NGIQYAEVSI SQIRDFRKNA QSQNHLFKLL HRGYTGLINS GEGDRGVAEC
PFDFYRTWVL DAEKARENVE KITRSTVGTA ECPIQGIPNE GKTKEIGV
