AMIA2_MYCTU
ID AMIA2_MYCTU Reviewed; 484 AA.
AC P9WQ99; L0TCA9; O05835; P63490;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Putative amidase AmiA2;
DE EC=3.5.1.4;
GN Name=amiA2; OrderedLocusNames=Rv2363; ORFNames=MTCY27.17c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP45151.1; -; Genomic_DNA.
DR PIR; B70586; B70586.
DR RefSeq; NP_216879.1; NC_000962.3.
DR RefSeq; WP_003412223.1; NZ_NVQJ01000029.1.
DR AlphaFoldDB; P9WQ99; -.
DR SMR; P9WQ99; -.
DR STRING; 83332.Rv2363; -.
DR PaxDb; P9WQ99; -.
DR DNASU; 888955; -.
DR GeneID; 45426350; -.
DR GeneID; 888955; -.
DR KEGG; mtu:Rv2363; -.
DR TubercuList; Rv2363; -.
DR eggNOG; COG0154; Bacteria.
DR OMA; NVLGWPS; -.
DR PhylomeDB; P9WQ99; -.
DR Proteomes; UP000001584; 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 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..484
FT /note="Putative amidase AmiA2"
FT /id="PRO_0000105253"
FT ACT_SITE 93
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 167
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 191
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 484 AA; 50884 MW; 90D86CCD0C90F02A CRC64;
MVGASGSDAG AISGSGNQRL PTLTDLLYQL ATRAVTSEEL VRRSLRAIDV SQPTLNAFRV
VLTESALADA AAADKRRAAG DTAPLLGIPI AVKDDVDVAG VPTAFGTQGY VAPATDDCEV
VRRLKAAGAV IVGKTNTCEL GQWPFTSGPG FGHTRNPWSR RHTPGGSSGG SAAAVAAGLV
TAAIGSDGAG SIRIPAAWTH LVGIKPQRGR ISTWPLPEAF NGVTVNGVLA RTVEDAALVL
DAASGNVEGD RHQPPPVTVS DFVGIAPGPL KIALSTHFPY TGFRAKLHPE ILAATQRVGD
QLELLGHTVV KGNPDYGLRL SWNFLARSTA GLWEWAERLG DEVTLDRRTV SNLRMGHVLS
QAILRSARRH EAADQRRVGS IFDIVDVVLA PTTAQPPPMA RAFDRLGSFG TDRAIIAACP
STWPWNLLGW PSINVPAGFT SDGLPIGVQL MGPANSEGML ISLAAELEAV SGWATKQPQV
WWTS