ID   AMIE_THISH              Reviewed;         347 AA.
AC   B8GQ39;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Aliphatic amidase {ECO:0000255|HAMAP-Rule:MF_01242};
DE            EC=3.5.1.4 {ECO:0000255|HAMAP-Rule:MF_01242};
DE   AltName: Full=Acylamide amidohydrolase {ECO:0000255|HAMAP-Rule:MF_01242};
GN   Name=amiE {ECO:0000255|HAMAP-Rule:MF_01242}; OrderedLocusNames=Tgr7_3117;
OS   Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-EbGR7;
RX   PubMed=21475584; DOI=10.4056/sigs.1483693;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA   Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL   Stand. Genomic Sci. 4:23-35(2011).
CC   -!- FUNCTION: Catalyzes the hydrolysis of short-chain aliphatic amides to
CC       their corresponding organic acids with release of ammonia.
CC       {ECO:0000255|HAMAP-Rule:MF_01242}.
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:0000255|HAMAP-Rule:MF_01242}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01242};
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Aliphatic amidase family. {ECO:0000255|HAMAP-Rule:MF_01242}.
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DR   EMBL; CP001339; ACL74186.1; -; Genomic_DNA.
DR   RefSeq; WP_012639648.1; NC_011901.1.
DR   AlphaFoldDB; B8GQ39; -.
DR   SMR; B8GQ39; -.
DR   STRING; 396588.Tgr7_3117; -.
DR   PRIDE; B8GQ39; -.
DR   EnsemblBacteria; ACL74186; ACL74186; Tgr7_3117.
DR   KEGG; tgr:Tgr7_3117; -.
DR   eggNOG; COG0388; Bacteria.
DR   HOGENOM; CLU_071797_0_0_6; -.
DR   OMA; PWVPIEG; -.
DR   OrthoDB; 1650683at2; -.
DR   Proteomes; UP000002383; Chromosome.
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   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..347
FT                   /note="Aliphatic amidase"
FT                   /id="PRO_1000165034"
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:0000255|HAMAP-Rule:MF_01242"
FT   ACT_SITE        134
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01242"
FT   ACT_SITE        166
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01242"
SQ   SEQUENCE   347 AA;  38826 MW;  067FDB7F366BCAA8 CRC64;
     MRHGDISSSK DCVGVAVVNY KMPRLHTRAE VLDNARKIAD MIVGMKQGLP GMDLVIFPEY
     STHGIMYDAK EMYDTASTIP GDETEIFADA CRRAKTWGVF SLTGEQHEDH PNKAPYNTLI
     LMNDKGEIVQ KYRKIMPWCP VEGWYPGDCT YVSEGPKGLK ISLIICDDGN YPEIWRDCTM
     RGAELVVRCQ GYMYPSKDQQ VIVSKAMAWM NNTYVAVANA TGFDGVYSYF GHSAIIGFDG
     RTLGECGEED YGIQYAELSV SQIRDFRKNA QSQNHLFKLL HRGYTGKINS GEGDQGVAEC
     PYEFYRTWIT SPDAAKEQVE AITRKTVGTA ECPIEGIPNE ETPSGHR