ID E3GF79_9FIRM Unreviewed; 395 AA.
AC E3GF79;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ADO38213.1};
GN OrderedLocusNames=ELI_3249 {ECO:0000313|EMBL:ADO38213.1};
OS Eubacterium callanderi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=53442 {ECO:0000313|EMBL:ADO38213.1, ECO:0000313|Proteomes:UP000006873};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KIST612;
RA Roh H., Ko H.-J., Kim D., Choi D.G., Park S., Kim S., Kim K.H., Chang I.S.,
RA Choi I.-G.;
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO38213.1, ECO:0000313|Proteomes:UP000006873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIST612 {ECO:0000313|EMBL:ADO38213.1,
RC ECO:0000313|Proteomes:UP000006873};
RX PubMed=21036996; DOI=10.1128/JB.01217-10;
RA Roh H., Ko H.J., Kim D., Choi D.G., Park S., Kim S., Chang I.S., Choi I.G.;
RT "Complete genome sequence of a carbon monoxide-utilizing acetogen,
RT Eubacterium limosum KIST612.";
RL J. Bacteriol. 193:307-308(2011).
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DR EMBL; CP002273; ADO38213.1; -; Genomic_DNA.
DR RefSeq; WP_013381523.1; NZ_QYRZ01000013.1.
DR AlphaFoldDB; E3GF79; -.
DR GeneID; 68364237; -.
DR KEGG; elm:ELI_3249; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_1_1_9; -.
DR Proteomes; UP000006873; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
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:SF98; N-ACETYLDIAMINOPIMELATE DEACETYLASE; 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;
FT DOMAIN 193..283
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 395 AA; 43783 MW; E3E76DF6BACB8C22 CRC64;
MAVDFYQKLP EAIKAYEPEA VSLRRALHKI PETGFNERET QAFIMDYLEK LGYTPEKVCD
TGVVLFIPSL NGLDETIAIR TDMDGLGVVE ETGVDFASEH EGMMHACGHD GHMSMVLLVA
RYLKEHPEAR VRNTLLVFQP AEEGPGGAGP IVESGVLEKY KAKAIFGYHL FPFVEEGLIS
TTPGPMMAMT SEFYIDILGK SGHAADPDQG IDAIVATADY ISGLQKIVSR TVSPNDSALL
SIGTINGGTR MNIIADKVIL SGTVRSFSED VQKAMKQRMV DMARGIEQMY HCRIEIRFVD
MYPPVINSEV LFDQIWPLCG EADEKKLFKK VMLAEDFAMY RKAIPGVFMG LGSGSEEKGY
TQNLHTHGFN FDEKVLLRGL QVYMNILTKA GEYTL
//
