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Database: UniProt
Entry: C6PUR5_9CLOT
LinkDB: C6PUR5_9CLOT
Original site: C6PUR5_9CLOT 
ID   C6PUR5_9CLOT            Unreviewed;       405 AA.
AC   C6PUR5;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:EET86994.1};
DE            EC=3.5.1.32 {ECO:0000313|EMBL:EET86994.1};
GN   ORFNames=CcarbDRAFT_2532 {ECO:0000313|EMBL:EET86994.1};
OS   Clostridium carboxidivorans P7.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536227 {ECO:0000313|EMBL:EET86994.1, ECO:0000313|Proteomes:UP000004198};
RN   [1] {ECO:0000313|EMBL:EET86994.1, ECO:0000313|Proteomes:UP000004198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P7 {ECO:0000313|EMBL:EET86994.1,
RC   ECO:0000313|Proteomes:UP000004198};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Hemme C.L.;
RT   "The draft genome of Clostridium carboxidivorans P7.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EET86994.1}.
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DR   EMBL; ACVI01000039; EET86994.1; -; Genomic_DNA.
DR   RefSeq; WP_007061417.1; NZ_GG770678.1.
DR   AlphaFoldDB; C6PUR5; -.
DR   STRING; 536227.Ccar_00245; -.
DR   KEGG; cck:Ccar_00245; -.
DR   PATRIC; fig|536227.13.peg.72; -.
DR   eggNOG; COG1473; Bacteria.
DR   OrthoDB; 9776731at2; -.
DR   Proteomes; UP000004198; Unassembled WGS sequence.
DR   GO; GO:0047980; F:hippurate hydrolase activity; IEA:UniProtKB-EC.
DR   CDD; cd03886; M20_Acy1; 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:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-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:EET86994.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004198}.
FT   DOMAIN          195..288
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   405 AA;  44242 MW;  593796495BDD66BB CRC64;
     MNSKIKSISE EIQDLLIRIR RNLHEIPELA FEEYHTSEMI ISELKKLKGM EISAGYAGGT
     GIVATLQGKK GKSDQCVMIR ADMDALPIEE NNDLAYCSKE KGKMHACGHD AHITWTLGAA
     MILTQLQESF SGTVKFVFQP AEEIAAGAIK MVEEKVLENP KVDIVLGAHG FPQYDTGKII
     IPQKNAFSAA RPLCIRVIGK GGHGSWPQDC VDPIAVANQI YMSLQQIISR KMKPADAAVL
     TIGSIHAGPK DKGNIIPNEC ILRGTLRHTT VNGMESMVQW VEGISQHIAA ANGAKVIVQC
     YHGVEPVIND KYCNKIFQKS AEEIVGKENV EMLEESNLGG EDFYHYSQKV KSVYFFVGCA
     PKNKVGTFSL HSSNFCIDES ILGTVAAVLS NTTISFLMNN NVGGN
//
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