ID Q8R5R5_CALS4 Unreviewed; 464 AA.
AC Q8R5R5;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase and related deacylases {ECO:0000313|EMBL:AAM24940.1};
GN Name=ArgE2 {ECO:0000313|EMBL:AAM24940.1};
GN OrderedLocusNames=TTE1746 {ECO:0000313|EMBL:AAM24940.1};
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068 {ECO:0000313|EMBL:AAM24940.1, ECO:0000313|Proteomes:UP000000555};
RN [1] {ECO:0000313|EMBL:AAM24940.1, ECO:0000313|Proteomes:UP000000555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4
RC {ECO:0000313|Proteomes:UP000000555};
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; AE008691; AAM24940.1; -; Genomic_DNA.
DR RefSeq; WP_011025942.1; NC_003869.1.
DR AlphaFoldDB; Q8R5R5; -.
DR STRING; 273068.TTE1746; -.
DR KEGG; tte:TTE1746; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_031786_2_0_9; -.
DR OrthoDB; 9761532at2; -.
DR Proteomes; UP000000555; Chromosome.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd03888; M20_PepV; 1.
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.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 4: Predicted;
KW Dipeptidase {ECO:0000256|ARBA:ARBA00022997};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022997};
KW Reference proteome {ECO:0000313|Proteomes:UP000000555};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 464 AA; 52173 MW; 6F49FB91FC01EA30 CRC64;
MDLNSYIDSM RDEIIKSVQE LVRIKSVQDE PKPGMPYGEG VARALEKALE IAERLGFKTK
NLDGYIGYAE YGEGEEMIAV LGHLDVVPEG DGWTYPPYGA EIHDGKIYGR GTVDDKGPII
AALYGLKAIK DAGLKLSKRV RIIFGTNEET GSHEIKYYLE HDEAPTMGFT PDAQYPIIHA
EKGITMFNVV KDFNKKPSRI VVKYIKGGER PNVVPGYCEA RLKVEEENTK KEILNELEAF
VRETGYDLKF EEKEGDLVIK SFGIPAHGSL PHLGKNAIMQ LFLFLDRINL DESDVKDFIH
FFATNVGMET NGKTFGIYLK DETGELTFNV GTVSIDEDKG VLGLNIRYPV KHKYEDWMNI
FEEKIKGQGM RIEDMLHQPP LYFPPDHPLI KILSKVYEEQ TGQKAELLAI GGGTYAKEMP
NTVAFGPVFP GKPELAHQAD EYIEIEDLIL NAKIYAHAIY ELAK
//
