ID D6E806_9ACTN Unreviewed; 475 AA.
AC D6E806;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Dipeptidase, putative {ECO:0000313|EMBL:CBL03853.1};
DE EC=3.5.1.18 {ECO:0000313|EMBL:CBL03853.1};
GN ORFNames=GPA_11710 {ECO:0000313|EMBL:CBL03853.1};
OS Gordonibacter pamelaeae 7-10-1-b.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Gordonibacter.
OX NCBI_TaxID=657308 {ECO:0000313|EMBL:CBL03853.1, ECO:0000313|Proteomes:UP000008805};
RN [1] {ECO:0000313|EMBL:CBL03853.1, ECO:0000313|Proteomes:UP000008805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Timmis K., Oxley A., Wurdemann D.;
RT "The genome sequence of Gordonibacter pamelaeae 7-10-1-bT.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL03853.1, ECO:0000313|Proteomes:UP000008805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RA Pajon A.;
RL Submitted (MAR-2010) 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; FP929047; CBL03853.1; -; Genomic_DNA.
DR RefSeq; WP_015539203.1; NC_021021.1.
DR AlphaFoldDB; D6E806; -.
DR GeneID; 78358204; -.
DR KEGG; gpa:GPA_11710; -.
DR PATRIC; fig|657308.3.peg.750; -.
DR HOGENOM; CLU_031786_0_0_11; -.
DR BioCyc; GPAM657308:GPA_RS05400-MONOMER; -.
DR Proteomes; UP000008805; Chromosome.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.70.360; -; 2.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR010964; M20A_pepV-rel.
DR InterPro; IPR002933; Peptidase_M20.
DR NCBIfam; TIGR01887; dipeptidaselike; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF33; DIPEPTIDASE SAOUHSC_01868-RELATED; 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 4: Predicted;
KW Dipeptidase {ECO:0000256|ARBA:ARBA00022997};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CBL03853.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022997};
KW Reference proteome {ECO:0000313|Proteomes:UP000008805};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 475 AA; 51464 MW; 02DF4874E395AD7B CRC64;
MDQTELTKKI DAYLEKNWDA MVDDIATLVR IPSFQEDDKK ADGAPFGPGP KKALAAALEL
AGGMGFTTHD AEGYIGFADF PGASDTQLGI IGHMDVVPAG PGWTFEPYEV TRKDGYLIGR
GTLDDKGPSV MALHAMKFWK DLQDQGEAPQ FPYTVRFLFG ANEESGMADV AYYHLHYDDP
AFLFTPDAEF PVCYGEKGGY DGMLMSKPIE PCARVIVEFE GGAATNAVPG LAHAIVNADA
HELKSTDRIV VTEAGPGRAR LEATGKGAHA SLPDDGINAI GLIVDYLLEN GLCGADERAF
LELDQKLLNH TDGSGVGIKS SDEYFGPLTV IGGTIALKDD RFVQTVDSRF PTSITADEIT
ERLRQLAEEI GGSFENTLLM EPFLVKPDSP VIQALLNAYN EATGEDAKPF TMGGGTYARE
FKSGASFGPE KPWEKNPDWV GTMHGPDEGV SEDLLRQSFK IYALTLDKLM QLDLK
//
