ID A4YTI3_BRASO Unreviewed; 432 AA.
AC A4YTI3;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Putative peptidase M20 family protein putative Acetylornithine deacetylase {ECO:0000313|EMBL:CAL77209.1};
DE EC=3.5.1.- {ECO:0000313|EMBL:CAL77209.1};
DE EC=3.5.1.16 {ECO:0000313|EMBL:CAL77209.1};
GN OrderedLocusNames=BRADO3421 {ECO:0000313|EMBL:CAL77209.1};
OS Bradyrhizobium sp. (strain ORS 278).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=114615 {ECO:0000313|EMBL:CAL77209.1, ECO:0000313|Proteomes:UP000001994};
RN [1] {ECO:0000313|EMBL:CAL77209.1, ECO:0000313|Proteomes:UP000001994}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ORS 278 {ECO:0000313|Proteomes:UP000001994};
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; CU234118; CAL77209.1; -; Genomic_DNA.
DR RefSeq; WP_011926359.1; NC_009445.1.
DR AlphaFoldDB; A4YTI3; -.
DR STRING; 114615.BRADO3421; -.
DR KEGG; bra:BRADO3421; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_0_0_5; -.
DR OrthoDB; 9809784at2; -.
DR Proteomes; UP000001994; Chromosome.
DR GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03895; M20_ArgE_DapE-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010182; ArgE/DapE.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR033687; YodQ-like.
DR NCBIfam; TIGR01910; DapE-ArgE; 1.
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 3: Inferred from homology;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAL77209.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001994}.
FT DOMAIN 210..322
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 432 AA; 46597 MW; 8E710CD52DC663D8 CRC64;
MTETVAAVPN DVMERLAAAV DANFKTQVAF LQQLVQFRSL RGEEAPVQDW LATEFEARGY
TVDRFSLADV DLMRHPKAAP MDTIALGGSK QVVATLDGAG KGRSLILQGH IDVVPEGPTD
LWSDAPYEAV VREGWMIGRG AQDMKAGVSA MIFALDAIKA AGFVPDGRIH VETVTEEEST
GNGALSTLLR GYTADACLIP EPTGHTLTRA QVGAIWFRLR VRGTPVHVAY AETGTNAILS
AMHLIRSFQE HTDEINARAT SNAWFAEVKN PIKFNVGIIK GGDWASSTPA WCDLDCRIGV
LPGETPAEAM AGIEQCLAKA QATDSFLSEN PVELVWSGFQ ADPAVCEPGS AAEAALADVH
ARVFEKPLEM RLSTAVNDTR YYAVDYGIPA LCYGPYGIGP HAFDERVDLD SVRKTTLSIA
MFVAQWCGLR KA
//
