AMI4_MYCBO
ID AMI4_MYCBO Reviewed; 475 AA.
AC P63497; A0A1R3Y466; O50404; X2BPC8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Putative amidase AmiD;
DE EC=3.5.1.4;
GN Name=amiD; OrderedLocusNames=BQ2027_MB3409;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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 -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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DR EMBL; LT708304; SIU02038.1; -; Genomic_DNA.
DR RefSeq; NP_857050.1; NC_002945.3.
DR RefSeq; WP_003417900.1; NC_002945.4.
DR AlphaFoldDB; P63497; -.
DR SMR; P63497; -.
DR EnsemblBacteria; SIU02038; SIU02038; BQ2027_MB3409.
DR PATRIC; fig|233413.5.peg.3745; -.
DR OMA; PAIWTIQ; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.1300.10; -; 1.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR PANTHER; PTHR11895; PTHR11895; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW Hydrolase.
FT CHAIN 1..475
FT /note="Putative amidase AmiD"
FT /id="PRO_0000105261"
FT ACT_SITE 93
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 166
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 190
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 475 AA; 50646 MW; 8A74C138EE3C6745 CRC64;
MTDADSAVPP RLDEDAISKL ELTEVADLIR TRQLTSAEVT ESTLRRIERL DPQLKSYAFV
MPETALAAAR AADADIARGH YEGVLHGVPI GVKDLCYTVD APTAAGTTIF RDFRPAYDAT
VVARLRAAGA VIIGKLAMTE GAYLGYHPSL PTPVNPWDPT AWAGVSSSGC GVATAAGLCF
GSIGSDTGGS IRFPTSMCGV TGIKPTWGRV SRHGVVELAA SYDHVGPITR SAHDAAVLLS
VIAGSDIHDP SCSAEPVPDY AADLALTRIP RVGVDWSQTT SFDEDTTAML ADVVKTLDDI
GWPVIDVKLP ALAPMVAAFG KMRAVETAIA HADTYPARAD EYGPIMRAMI DAGHRLAAVE
YQTLTERRLE FTRSLRRVFH DVDILLMPSA GIASPTLETM RGLGQDPELT ARLAMPTAPF
NVSGNPAICL PAGTTARGTP LGVQFIGREF DEHLLVRAGH AFQQVTGYHR RRPPV