ID C5BFE2_EDWI9 Unreviewed; 426 AA.
AC C5BFE2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Amidohydrolase, putative {ECO:0000313|EMBL:ACR68659.1};
GN OrderedLocusNames=NT01EI_1473 {ECO:0000313|EMBL:ACR68659.1};
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR68659.1, ECO:0000313|Proteomes:UP000001485};
RN [1] {ECO:0000313|Proteomes:UP000001485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACR68659.1, ECO:0000313|Proteomes:UP000001485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146 {ECO:0000313|EMBL:ACR68659.1,
RC ECO:0000313|Proteomes:UP000001485};
RX PubMed=22247535; DOI=10.1128/JB.06522-11;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA Lawrence M.L.;
RT "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated with
RT a Natural Channel Catfish Outbreak of Enteric Septicemia of Catfish.";
RL J. Bacteriol. 194:740-741(2012).
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DR EMBL; CP001600; ACR68659.1; -; Genomic_DNA.
DR RefSeq; WP_015870822.1; NC_012779.2.
DR AlphaFoldDB; C5BFE2; -.
DR STRING; 67780.B6E78_00620; -.
DR GeneID; 69538465; -.
DR KEGG; eic:NT01EI_1473; -.
DR PATRIC; fig|634503.3.peg.1321; -.
DR HOGENOM; CLU_023257_2_1_6; -.
DR OrthoDB; 9777385at2; -.
DR Proteomes; UP000001485; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR CDD; cd05665; M20_Acy1_IAAspH; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR033845; AbgA.
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; PTHR30575:SF3; M20_DIMER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR30575; PEPTIDASE M20; 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:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACR68659.1}.
FT DOMAIN 224..297
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 426 AA; 45784 MW; 1CA01C8C20FC5295 CRC64;
MTISDPEQLR RWRRMFHQIP ETGWSEFITS ARLIEMLRAM GYRVLPGSAF LSRAHIQGRN
DDEVARGLDR ARRYPVSDAL LEEMGDLTGC VALLETGRPG PTVALRFDID CVAVTESGAP
QHPPRAADFA SRHPGCMHAC GHDGHMAIGL GVAQALYALR DQLCGTVKLL FQPAEEGVRG
ARPVAEGGLL DDVDYFLSAH IGMGVPSGEI VVDPRDFLCT TKLDLRFFGA PAHAGMMPQG
GANALAGACH CVTQLLGIPR HGDGMSRINI GTLRAGEGRN VIPAYAEMQL EVRGANRTIN
DYMAQQVLRI AEGAAQSFGL RVEHQVMGSA VDLHNDAALM TLVADIASQQ QDLRIGEASF
GGSEDATLLV ERVQAHGGQA VYLVLGADLR AGHHQSGFDF DEAVLSRGCA LFTACVSRLC
RTVQPA
//
