ID   Q73Y15_MYCPA            Unreviewed;       503 AA.
AC   Q73Y15;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=amidase {ECO:0000256|ARBA:ARBA00012922};
DE            EC=3.5.1.4 {ECO:0000256|ARBA:ARBA00012922};
GN   Name=amiA2 {ECO:0000313|EMBL:AAS04460.1};
GN   OrderedLocusNames=MAP_2143 {ECO:0000313|EMBL:AAS04460.1};
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316 {ECO:0000313|EMBL:AAS04460.1, ECO:0000313|Proteomes:UP000000580};
RN   [1] {ECO:0000313|EMBL:AAS04460.1, ECO:0000313|Proteomes:UP000000580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10 {ECO:0000313|Proteomes:UP000000580};
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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:0000256|ARBA:ARBA00001311};
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DR   EMBL; AE016958; AAS04460.1; -; Genomic_DNA.
DR   RefSeq; WP_003872519.1; NZ_CP106873.1.
DR   AlphaFoldDB; Q73Y15; -.
DR   STRING; 262316.MAP_2143; -.
DR   KEGG; mpa:MAP_2143; -.
DR   PATRIC; fig|262316.17.peg.2278; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_4_11; -.
DR   Proteomes; UP000000580; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   PANTHER; PTHR11895:SF180; AMIDASE AMIC-RELATED; 1.
DR   PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000580}.
FT   DOMAIN          45..464
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   503 AA;  52197 MW;  F060F65FF28EC991 CRC64;
     MIGASESGPG ALSGSGSGSG NQRLPTLTDL LYQLASRSVS STTLVGRSLH AIHASQPTLN
     AFRVVLTESA LADAAEADRR RAAGDTAPLL GIPIAVKDDV DIAGVPTAFG TEGSVPPATH
     DAEVVRRLKA AGAVIVGKTN TCELGQWPFT SGPGFGHTRN PWSRRHTPGG SSGGSAAAVA
     AGLVTAAIGS DGAGSIRIPA AWTHLVGIKP QRGRISTWPL PEAFNGITVN GVLARTVADA
     ALVLDAASGN VDGDRHKPPP ITASDYVGKA PGPLNIALST RFPYTGFRPK LHPEILAATR
     AVGKQLELLG HTVVPGNPDY GMRLSWDFLA RSTAGLRDWE ERLGDGVVLD PRTVANLRLG
     HLLGQAILRS ARRHEAADQR RVGSIFDIVD VVLAPTTAQP PPLARAFDRL SGFGTDRAMI
     AACPLTFPWN VLGWPSINVP AGFTSDGLPI GVQLMGPANS EGMLISLAAE LEAVSGWASK
     QPQPWWDQSA DTPPAPGQPA PTG
//