ID A0A061LTC3_9MICO Unreviewed; 448 AA.
AC A0A061LTC3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:EYT51786.1};
GN ORFNames=H490_0114615 {ECO:0000313|EMBL:EYT51786.1};
OS Leucobacter sp. UCD-THU.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1292023 {ECO:0000313|EMBL:EYT51786.1, ECO:0000313|Proteomes:UP000026917};
RN [1] {ECO:0000313|EMBL:EYT51786.1, ECO:0000313|Proteomes:UP000026917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-THU {ECO:0000313|EMBL:EYT51786.1,
RC ECO:0000313|Proteomes:UP000026917};
RX PubMed=23792744; DOI=10.1128/genomeA.00325-13;
RA Holland-Moritz H.E., Bevans D.R., Lang J.M., Darling A.E., Eisen J.A.,
RA Coil D.A.;
RT "Draft Genome Sequence of Leucobacter sp. Strain UCD-THU (Phylum
RT Actinobacteria).";
RL Genome Announc. 1:S69-S82(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:EYT51786.1}.
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DR EMBL; APJM01000028; EYT51786.1; -; Genomic_DNA.
DR RefSeq; WP_017882600.1; NZ_APJM01000028.1.
DR AlphaFoldDB; A0A061LTC3; -.
DR STRING; 1292023.H490_0114615; -.
DR HOGENOM; CLU_021802_11_2_11; -.
DR OrthoDB; 7055905at2; -.
DR Proteomes; UP000026917; 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; 1.10.150.900; -; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
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 PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF32; CONSERVED PROTEIN; 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 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000026917};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 198..343
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 448 AA; 47574 MW; 13C1717A4F4F87A7 CRC64;
MTEERIDGSG GAGEAIELLR ELIREGCVND GTPSSGQEIR NVRVLQRFLA DAIALGRIET
QVLESAPGRA SLVARVRGTD PDAPALGLLG HLDVVPVDPD GWTRNPFGGE LIDGEVWGRG
AVDMLYLTAA FACVLREVAL APRPPRGDLV LLAVADEEAG SDLGMHWLVR EHPEAVRVTE
ALSESGGMRM GRHVAIEVAE KGSAGRRLVV RGKPGHASIP FGATSAAYRM GEVLQRLEAV
MPAAQLGELW NAFVDARIDD PELAERLRDP VRLDAALPQL GGIAGYAHAV SRITISPTVV
RAGAAHNVIP GSASIDLDIR TLPGTSDEEV DELIAAVLGP LADEVEIRRL RGWAATGSRS
DTPLFAAIKR AIAEVADAPT VPIMAAGGSD ARVLRELGIP AYGFGLLAPG WSYERYREGV
HGNDERIDLT SIELSMAALR SIVSERIG
//
