ID G8PNB5_PSEUV Unreviewed; 437 AA.
AC G8PNB5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:AEV37032.1};
DE EC=3.-.-.- {ECO:0000313|EMBL:AEV37032.1};
GN OrderedLocusNames=PSE_2524 {ECO:0000313|EMBL:AEV37032.1};
OS Pseudovibrio sp. (strain FO-BEG1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Stappiaceae; Pseudovibrio.
OX NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV37032.1, ECO:0000313|Proteomes:UP000005634};
RN [1] {ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT interacting bacteria.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV37032.1, ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV37032.1,
RC ECO:0000313|Proteomes:UP000005634};
RX PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT for symbiosis.";
RL Environ. Microbiol. 15:2095-2113(2013).
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; CP003147; AEV37032.1; -; Genomic_DNA.
DR RefSeq; WP_008549953.1; NC_016642.1.
DR AlphaFoldDB; G8PNB5; -.
DR STRING; 911045.PSE_2524; -.
DR KEGG; psf:PSE_2524; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_2_3_5; -.
DR Proteomes; UP000005634; 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; IPR010182; ArgE/DapE.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEV37032.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 196..314
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT COILED 300..331
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 437 AA; 48166 MW; D195244DF7A09C60 CRC64;
MRDELRQSVE SKVEELVALT RDLIAFPTIN PPGEAYRPCA EFIGERLRRK GFQVEYVRGE
STPGDSDRYP RINVICRYEG RGPGPCVHFN SHIDVVEVGY GWTVDPFAGV VKDGKVFGRG
ACDMKGGLAS SIIAAETLIE CFPEFCGAIE ISGTVDEESG GLGGVAYLAR HGYFSKPRVD
HVIIPEPLHK DQVCLGHRGV WWSEIETRGS IAHGSMPFLG DSAIRHMGAF LNVLEDELYP
ALSKKQTQMP VIPPGARSST LNINSLHGGQ DEGHDGLPSP CVADSCRIVL DRRFLIEEPL
EDVKQEIVEI LENLRKTRRN FEYELKDLLE VLPVMADKDS PVARAVADGI KDVLQKDASY
VVSPGTYDQK HITRLGHLHD CIAYGPGKLE MAHRPDEFVG IEDLVDSAKV MALAAYSLLT
EPDASPITRT QSDHVHS
//
