ID C5T8M8_ACIDE Unreviewed; 401 AA.
AC C5T8M8;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:EER59167.1};
DE EC=3.5.1.32 {ECO:0000313|EMBL:EER59167.1};
GN ORFNames=AcdelDRAFT_3258 {ECO:0000313|EMBL:EER59167.1};
OS Acidovorax delafieldii 2AN.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=573060 {ECO:0000313|EMBL:EER59167.1, ECO:0000313|Proteomes:UP000003856};
RN [1] {ECO:0000313|EMBL:EER59167.1, ECO:0000313|Proteomes:UP000003856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2AN {ECO:0000313|EMBL:EER59167.1,
RC ECO:0000313|Proteomes:UP000003856};
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., Shelobolina E.S.,
RA Picardal F., Roden E., Emerson D.;
RT "The draft genome of Acidovorax delafieldii 2AN.";
RL Submitted (MAY-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:EER59167.1}.
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DR EMBL; ACQT01000155; EER59167.1; -; Genomic_DNA.
DR RefSeq; WP_005798599.1; NZ_ACQT01000155.1.
DR AlphaFoldDB; C5T8M8; -.
DR PATRIC; fig|573060.9.peg.1770; -.
DR OrthoDB; 8875216at2; -.
DR Proteomes; UP000003856; Unassembled WGS sequence.
DR GO; GO:0047980; F:hippurate hydrolase activity; IEA:UniProtKB-EC.
DR CDD; cd05666; 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: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:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EER59167.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003856}.
FT DOMAIN 188..284
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 401 AA; 43019 MW; A20A2CF5E7F9C49C CRC64;
MNVIDSIVTQ AASIAAVRRD IHAHPELCFE EVRTADVVAQ KLTEWGIPIH RGLGKTGVVG
IVRGRDGGAS GRAIGLRADM DALPMQEFNT FAHASQHPGK MHACGHDGHT AMLLAAAQHF
AKHRNFDGTV YLIFQPAEEG GGGARVMIED GLFEQFPMQA VFGMHNWPGM PVGTLAVSPG
PVMASSNEFK ITIRGKGGHA ALPHTGIDPV PIACQMVQAF QTIISRNKKP VDAGVISVTM
IHAGEASNVV PDSCELQGTV RTFTIEVLDL IEKRMKQVAE HTCAAHEATC EFEFVRNYPP
TVNSAAEAEF ARKVMAGIVG EAHVLVQEPT MGAEDFAFML QAKPGAYCFI ANGEGAHREM
GHGGGPCTLH NPSYDFNDDL IPLGATYWVR LAEEWLSAPA A
//
