ID U4KSZ5_9MOLU Unreviewed; 458 AA.
AC U4KSZ5;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:CCV65799.1};
DE EC=3.5.1.16 {ECO:0000313|EMBL:CCV65799.1};
GN Name=argE {ECO:0000313|EMBL:CCV65799.1};
GN ORFNames=BN85307780 {ECO:0000313|EMBL:CCV65799.1};
OS Paracholeplasma brassicae.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Paracholeplasma.
OX NCBI_TaxID=61635 {ECO:0000313|EMBL:CCV65799.1, ECO:0000313|Proteomes:UP000032737};
RN [1] {ECO:0000313|EMBL:CCV65799.1, ECO:0000313|Proteomes:UP000032737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0502 {ECO:0000313|Proteomes:UP000032737};
RX PubMed=24158107; DOI=10.1159/000354322;
RA Kube M., Siewert C., Migdoll A.M., Duduk B., Holz S., Rabus R.,
RA Seemuller E., Mitrovic J., Muller I., Buttner C., Reinhardt R.;
RT "Analysis of the Complete Genomes of Acholeplasma brassicae , A. palmae and
RT A. laidlawii and Their Comparison to the Obligate Parasites from '
RT Candidatus Phytoplasma'.";
RL J. Mol. Microbiol. Biotechnol. 24:19-36(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; FO681348; CCV65799.1; -; Genomic_DNA.
DR RefSeq; WP_030004662.1; NC_022549.1.
DR AlphaFoldDB; U4KSZ5; -.
DR STRING; 61635.BN85307780; -.
DR KEGG; abra:BN85307780; -.
DR HOGENOM; CLU_031786_2_0_14; -.
DR OrthoDB; 9761532at2; -.
DR Proteomes; UP000032737; Chromosome Acholeplasma brassicae.
DR GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC.
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.
PE 4: Predicted;
KW Dipeptidase {ECO:0000256|ARBA:ARBA00022997};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCV65799.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022997};
KW Reference proteome {ECO:0000313|Proteomes:UP000032737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 458 AA; 51107 MW; 9A19B5CCD7AAEA86 CRC64;
MSIDFRKEVE KRKEAILKDL TEIIQINSEL TTFDEKRVNA PFGEGIDEAL TFMLNLGKRD
GFNTLNAEHY AGHIEYGNQE EYVGMIGHLD VVPAGSGWSY PPYGAVIADG KMYGRGTEDD
KGPTIAAYYA MKILKDLDLP LSKRIKLILG TDEETAWRGV KYYFNQYPEQ PVAGFIPDSD
FPLTYAEKGI LRVVVRGKAD DSVLHSFEAG LRDNMVPDQA KAVLNNVELE KKYLEFLEKR
NLEGSAVVND GKLELEINGI SAHGSTPQLG VNAAYLLVHF FNEVGISNAF IDAINTYLLD
DPVGKKLGVD FVEKEMGSVT INAGVFNFNQ GKFEIVLNPR YPHGVDYDAF IDKISRGFES
LGAQVEIGKH QKLLYVDPNS EMIQKLMGVY KKYTNDVEAK PMTTGGGTFA RAMKNSVAFG
PHFPGKPTYI HQKNEYIILE DFFLSIAIYA EALFELAK
//
