ID C6PN03_9CLOT Unreviewed; 391 AA.
AC C6PN03;
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:EET89336.1};
DE EC=3.5.1.32 {ECO:0000313|EMBL:EET89336.1};
GN ORFNames=CcarbDRAFT_0170 {ECO:0000313|EMBL:EET89336.1};
OS Clostridium carboxidivorans P7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536227 {ECO:0000313|EMBL:EET89336.1, ECO:0000313|Proteomes:UP000004198};
RN [1] {ECO:0000313|EMBL:EET89336.1, ECO:0000313|Proteomes:UP000004198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P7 {ECO:0000313|EMBL:EET89336.1,
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:EET89336.1}.
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DR EMBL; ACVI01000002; EET89336.1; -; Genomic_DNA.
DR RefSeq; WP_007059055.1; NZ_GG770683.1.
DR AlphaFoldDB; C6PN03; -.
DR KEGG; cck:Ccar_08560; -.
DR PATRIC; fig|536227.13.peg.1795; -.
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 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:EET89336.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004198}.
FT DOMAIN 189..284
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 391 AA; 43252 MW; B2FA1414E013CF93 CRC64;
MNTDMLKKAR EIQDWVVKFR RDFHKHPEQS FKEFRTSKIV SEELTKMGIK VEHIGETGVI
GILEGASKEK VIALRADMDA LSVTEDTGLP FSSENVGFMH GCGHDCHTSM LLGAAKLLSE
VKDQLNGTVK FIFQPAEEVA AGAKKLVEGG VLKNPDVDFI FGMHIWSDIP VGKVVLKEGP
FMASGDIWDL TIKGKSCHGS SPWQGVDAIV CASAVINGIQ SIVSRINDVR SPIVINIGTI
HGGERFNVTP GSVKMEGMNR AFSTYTRKKI PEWVEKIVKS TCEAYGCDYE YNYNFICATT
TNDEKCTKFA KKSIEKFLGE DKIMSCEKIM GSEDMSEYLE HVPGTLMLLG GRNEAKNCCY
SHHSNHFNVD EDALPIGVAS YAQIAIDYLC K
//
