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AMI4_MYCTO
ID   AMI4_MYCTO              Reviewed;         475 AA.
AC   P9WQ92; L0TF69; O50404; P63496;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Putative amidase AmiD;
DE            EC=3.5.1.4;
GN   Name=amiD; OrderedLocusNames=MT3485;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK47821.1; -; Genomic_DNA.
DR   PIR; F70972; F70972.
DR   RefSeq; WP_003417900.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQ92; -.
DR   SMR; P9WQ92; -.
DR   EnsemblBacteria; AAK47821; AAK47821; MT3485.
DR   KEGG; mtc:MT3485; -.
DR   PATRIC; fig|83331.31.peg.3742; -.
DR   HOGENOM; CLU_009600_0_3_11; -.
DR   Proteomes; UP000001020; 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_0000426816"
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
 
 
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