ID A0A0P1IPN7_9RHOB Unreviewed; 382 AA.
AC A0A0P1IPN7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
GN Name=argE_2 {ECO:0000313|EMBL:CUK25538.1};
GN ORFNames=TA5114_01339 {ECO:0000313|EMBL:CUK25538.1};
OS Cognatishimia activa.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cognatishimia.
OX NCBI_TaxID=1715691 {ECO:0000313|EMBL:CUK25538.1, ECO:0000313|Proteomes:UP000051184};
RN [1] {ECO:0000313|Proteomes:UP000051184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5114 {ECO:0000313|Proteomes:UP000051184};
RA Rodrigo-Torres Lidia, Arahal R.David.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; CYUE01000013; CUK25538.1; -; Genomic_DNA.
DR RefSeq; WP_058314520.1; NZ_CYUE01000013.1.
DR AlphaFoldDB; A0A0P1IPN7; -.
DR STRING; 1715691.TA5113_01599; -.
DR OrthoDB; 9809784at2; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000051184; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR010182; ArgE/DapE.
DR InterPro; IPR001261; ArgE/DapE_CS.
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.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CUK25538.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000051184};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 171..278
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 382 AA; 39929 MW; EAD8C12FB587FAF3 CRC64;
MSEVITLLSQ LVRIDSVNPS LSDGGAGESQ AADFVGEWFQ TRGFDVTRLE STSGRPSIVA
VAKGTGGGKT LMFNGHLDTV SVESYDGDPF DPKLADGWLY GRGSADMKSG VAAMMIAASR
AAQSGLAGDI IVTCVADEEH ASLGTQEVIA AGYHADAAVV PEPVGHKIVA AHKGFIWFDL
VFEGVAAHGS NPDKGVDAIV KAGKFLVALE NYAAELAQQA VHPLVGVPSV HASLIKGGVE
MSSYPAQCKL SIERRTLPRE TPDEVEAEIE QLLNNLGSAD PAFKATLKRG LVRLPYECVQ
GAEIIDVATR SILNATGRPA EIAGMNGWTD CALLGEAGIP AILVGPEGRG GHSKCESVSI
QSVETLTDIL FQIATDFCAT EA
//
