ID Q9HTY4_PSEAE Unreviewed; 384 AA.
AC Q9HTY4;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:AAG08591.1};
GN Name=argE {ECO:0000313|EMBL:AAG08591.1};
GN OrderedLocusNames=PA5206 {ECO:0000313|EMBL:AAG08591.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964 {ECO:0000313|EMBL:AAG08591.1, ECO:0000313|Proteomes:UP000002438};
RN [1] {ECO:0000313|EMBL:AAG08591.1, ECO:0000313|Proteomes:UP000002438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC 1C / PRS 101 / PAO1 {ECO:0000313|Proteomes:UP000002438};
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.Q., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R., Smith K.,
RA Spencer D., Wong G.K., Wu Z., Paulsen I.T., Reizer J., Saier M.H.,
RA Hancock R.E., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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DR EMBL; AE004091; AAG08591.1; -; Genomic_DNA.
DR PIR; A82996; A82996.
DR RefSeq; NP_253893.1; NC_002516.2.
DR RefSeq; WP_003114054.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HTY4; -.
DR SMR; Q9HTY4; -.
DR STRING; 208964.PA5206; -.
DR PaxDb; 208964-PA5206; -.
DR DNASU; 879575; -.
DR GeneID; 879575; -.
DR KEGG; pae:PA5206; -.
DR PATRIC; fig|208964.12.peg.5456; -.
DR PseudoCAP; PA5206; -.
DR HOGENOM; CLU_021802_2_4_6; -.
DR InParanoid; Q9HTY4; -.
DR OrthoDB; 3665926at2; -.
DR PhylomeDB; Q9HTY4; -.
DR BioCyc; PAER208964:G1FZ6-5325-MONOMER; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008777; F:acetylornithine deacetylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR CDD; cd03894; M20_ArgE; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010169; AcOrn-deacetyl.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01892; AcOrn-deacetyl; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF1; ACETYLORNITHINE DEACETYLASE; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002438}.
FT DOMAIN 175..284
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 384 AA; 42163 MW; FD00DF19C8DEA9AC CRC64;
MPLPSLKDQF GALIAASSVS CTQPELDQTN RPVVDLLASW LGDLGFRCEI REVSPGKFNL
LASYGSGPGG LVLAGHTDTV PYDEALWSSD PLRLDERDGR WYGLGSCDMK GFFPLAIEAL
LPLLDQPFRQ PLMILATCDE ESSMAGARAL AESGRPLGRA TVIGEPTNLR PIRLHKGVMM
ERIEILGQSG HSSDPNLGRS ALEAMHATIG ELMALRGEWQ RAWNNPQFSV PQPTLNFGCI
HGGDNPNRIC GQCSLEFDLR PLPGMQPKQL REAIRQRLRP LAERHQVSID YQPLFPAVPP
FEQAQDSELV RVAERLTGHR AEAVAFGTEA PYFQRLGSET LVLGAGDIAC AHQPDEHLEL
ARIEPMVGVL RRLIQHYCLT PAAD
//