ID A0A0A0EJH5_9RHOB Unreviewed; 434 AA.
AC A0A0A0EJH5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:KGM50288.1};
GN ORFNames=ATO9_01985 {ECO:0000313|EMBL:KGM50288.1};
OS Pseudooceanicola atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=1461694 {ECO:0000313|EMBL:KGM50288.1, ECO:0000313|Proteomes:UP000030004};
RN [1] {ECO:0000313|EMBL:KGM50288.1, ECO:0000313|Proteomes:UP000030004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-s11g {ECO:0000313|EMBL:KGM50288.1,
RC ECO:0000313|Proteomes:UP000030004};
RX PubMed=25663028; DOI=10.1007/s10482-015-0398-2;
RA Lai Q., Li G., Liu X., Du Y., Sun F., Shao Z.;
RT "Pseudooceanicola atlanticus gen. nov. sp. nov., isolated from surface
RT seawater of the Atlantic Ocean and reclassification of Oceanicola
RT batsensis, Oceanicola marinus, Oceanicola nitratireducens, Oceanicola
RT nanhaiensis, Oceanicola antarcticus and Oceanicola flagellatus, as
RT Pseudooceanicola batsensis comb. nov., Pseudooceanicola marinus comb. nov.,
RT Pseudooceanicola nitratireducens comb. nov., Pseudooceanicola nanhaiensis
RT comb. nov., Pseudooceanicola antarcticus comb. nov., and Pseudooceanicola
RT flagellatus comb. nov.";
RL Antonie Van Leeuwenhoek 107:1065-1074(2015).
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}.
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:KGM50288.1}.
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DR EMBL; AQQX01000001; KGM50288.1; -; Genomic_DNA.
DR RefSeq; WP_043744317.1; NZ_CP051248.1.
DR AlphaFoldDB; A0A0A0EJH5; -.
DR STRING; 1461694.ATO9_01985; -.
DR eggNOG; COG0624; Bacteria.
DR OrthoDB; 9809784at2; -.
DR Proteomes; UP000030004; Unassembled WGS sequence.
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; 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 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030004}.
FT DOMAIN 202..323
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 434 AA; 47747 MW; 36705AD5CC7A9D6B CRC64;
MPDTALTDLQ TRLSDEIAAR RDDLTALTQD LIRIPTLNPP GENYREICDF LDRRLLRSGF
HTELIRAEGS PGDSEKYPRW NIVARREGNR PGECVHFNSH IDVVDVGKGW TTDPFGGEVK
DGKVYGRGAC DMKGGLAASI VAAEAFLAVV PDWQGAIEIS GTADEESGGF GGVAYLAEKG
HFERVDHVII PEPLNVDRIC LGHRGVWWAE IETHGEIAHG SMPFLGDCAV RHMGAVLHEM
EETLFPALAR KRTDMPVVPE GARQSTLNIN SLHGGQAEIA KDSTGLPSPV VPDSARMVID
RRFLIEEDID EVQGEIRDVL ERVRANRENF AYDIREMHRV LPTMTDRQAP VVTTVEAAIR
KTLSKDPDFV VSPGTYDQKH IDRIGKLKNC IAYGPGILDL AHKPDEYVGI DDMVASAQVM
ALSLLSLLGP PQTP
//
