ID A6TSC3_ALKMQ Unreviewed; 388 AA.
AC A6TSC3;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ABR49091.1};
DE EC=3.5.1.14 {ECO:0000313|EMBL:ABR49091.1};
GN OrderedLocusNames=Amet_2941 {ECO:0000313|EMBL:ABR49091.1};
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR49091.1, ECO:0000313|Proteomes:UP000001572};
RN [1] {ECO:0000313|Proteomes:UP000001572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX PubMed=27811105; DOI=10.1128/genomeA.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000724; ABR49091.1; -; Genomic_DNA.
DR RefSeq; WP_012064059.1; NC_009633.1.
DR AlphaFoldDB; A6TSC3; -.
DR STRING; 293826.Amet_2941; -.
DR KEGG; amt:Amet_2941; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_9; -.
DR OrthoDB; 9776731at2; -.
DR Proteomes; UP000001572; Chromosome.
DR GO; GO:0004046; F:aminoacylase activity; IEA:UniProtKB-EC.
DR CDD; cd08019; M20_Acy1-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF166; AMIDOHYDROLASE YHAA-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ABR49091.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001572}.
FT DOMAIN 185..280
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 388 AA; 42267 MW; 1079CD5F89460ADF CRC64;
MEIKDVVKKY NDYVIQMRRD FHMNPESSWE EFRTSGIVKA ELDKLSIPYI SVAGTGVVAT
IKGIGAGKIV ALRADMDALE IEETNDVPYK SKFPGKMHAC GHDGHTAMLL GAAKVFNEMK
HEINGTVKLI FQPAEEVAAG ARKMLDESNF MDDVDGSFAI HLWSGIEVGK ISIEAGPRMA
SADIFEIIIN GKSGHGSMPH QAIDAVVAAS AVVMDLQSVV SREFSPLDSV VLSIGSFHAG
TRFNIIANKA ILSGTTRCFK NKIRDMLPSV MERIVKNTAA SYRAEATLKY TPGTPPTIND
PTCAKIAAGS VEKILGENGV VEMEKTTGGE DFALFLNKAP GVMAFVGMRN EEKDACYAHH
HERFNMDEDA LEIGTALYVQ YALDFLNN
//
