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Database: UniProt
Entry: H5YQM6_9BRAD
LinkDB: H5YQM6_9BRAD
Original site: H5YQM6_9BRAD 
ID   H5YQM6_9BRAD            Unreviewed;       432 AA.
AC   H5YQM6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Acetylornithine deacetylase/succinyldiaminopimelate desuccinylase-like deacylase {ECO:0000313|EMBL:EHR05132.1};
GN   ORFNames=Bra471DRAFT_05945 {ECO:0000313|EMBL:EHR05132.1};
OS   Bradyrhizobium sp. WSM471.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=319017 {ECO:0000313|EMBL:EHR05132.1};
RN   [1] {ECO:0000313|EMBL:EHR05132.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM471 {ECO:0000313|EMBL:EHR05132.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA   Howieson J., Reeve W., Woyke T.;
RT   "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; CM001442; EHR05132.1; -; Genomic_DNA.
DR   RefSeq; WP_007613604.1; NZ_CM001442.1.
DR   AlphaFoldDB; H5YQM6; -.
DR   HOGENOM; CLU_021802_2_0_5; -.
DR   OrthoDB; 9809784at2; -.
DR   Proteomes; UP000005774; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF3; ACETYLORNITHINE DEACETYLASE-RELATED; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          215..317
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   432 AA;  47258 MW;  ACB141F269240C0E CRC64;
     MQMPVTPPYS DLEQRVLSRI TEERWLELAS ELIRTGQPRS GNPLDPDLPP AEEEAISMLV
     AGKLEALGME VTKHSAQPHR PNVLGVLKGR DGGPSLILND HLDTYPAVEP EKWHMTDFDP
     FKATRHGDLL YARGTSDTRG NLAASLLAVQ ALTEAGVKFD GTLMCCYTVD EERNGTEGSI
     YMLNKVGLTA DYEITAEPTA WGDVNTDWGM NLSVANSGHC LIELTVHGIK SHIWRPDISV
     NAIMEAAKLL PKLKDMAFTH VPSKFMGHTP PCCAVVRIRS GLPGEMQFSP DACTITLAVV
     GIVPGMTLSS VIGDIERLGR ETFAGVNDVK VEVRQVPGSL FVNATEPVPV EEEPCRSLRA
     VYRRLMGREP GVNRKNAFND TIRFREAGIN AVTFGPGEDG WAVDNENISI TKSVMATRIY
     ALTIMQILGV RT
//
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