ID E8RP29_ASTEC Unreviewed; 439 AA.
AC E8RP29;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ADU12999.1};
DE EC=3.5.1.32 {ECO:0000313|EMBL:ADU12999.1};
GN OrderedLocusNames=Astex_1326 {ECO:0000313|EMBL:ADU12999.1};
OS Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / KCTC 12464 /
OS NCIMB 9791 / VKM B-1370 / CB 48).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=573065 {ECO:0000313|EMBL:ADU12999.1, ECO:0000313|Proteomes:UP000001492};
RN [1] {ECO:0000313|Proteomes:UP000001492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15261 / DSM 4724 / KCTC 12464 / NCIMB 9791 / VKM B-1370 /
RC CB 48 {ECO:0000313|Proteomes:UP000001492};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Brun Y.V., Woyke T.;
RT "Complete sequence of chromosome 1 of Asticcacaulis excentricus CB 48.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002395; ADU12999.1; -; Genomic_DNA.
DR RefSeq; WP_013478831.1; NC_014816.1.
DR AlphaFoldDB; E8RP29; -.
DR STRING; 573065.Astex_1326; -.
DR KEGG; aex:Astex_1326; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_6_0_5; -.
DR OrthoDB; 9777385at2; -.
DR Proteomes; UP000001492; Chromosome 1.
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:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADU12999.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001492};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..439
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003229937"
FT DOMAIN 218..307
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 439 AA; 46342 MW; A78476E6FFC36A63 CRC64;
MRRLLPVLTA ALMGLPLPAL AEPDYVAAIR ADYQKDLGDM WDWFHRNPEL SMLESKTAAR
MAKELRATGA EVTEKVGGTG VVAVIRNGPG PVVMLRADMD GLPVKEASGL PNASVAKQVG
TDGVEYPVMH ACGHDTHITA MVATVRQLQR LKSQWKGTLV IVIQPGEERV MGAKAMLKDG
LYIRFPKPDY ALAFHVNSQM PAGKVAASEN IQYSSSDSID IHVHGVGAHG ASPHLGKDPV
YIGSQIVIAL QGLISRERSP LSPGVITVGA FHAGSKHNII SDAAELQVTV RANDEVTRGQ
LVDGVKRVAV NMGRVNGLPD DKLPEVNVVE GTPTTINDAA LARRLNGAIA AALGPNTVVP
FQQMGMGAED FAYFVQPDLK VPGYYFAVGG TPQAAFDAAR AGGPAVASHH SALFKIDPEA
TIVTGASAMT AAALDLLKP
//
