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Database: UniProt
Entry: A0A0Q5PTU1_9BURK
LinkDB: A0A0Q5PTU1_9BURK
Original site: A0A0Q5PTU1_9BURK 
ID   A0A0Q5PTU1_9BURK        Unreviewed;       340 AA.
AC   A0A0Q5PTU1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Acetylpolyamine aminohydrolase {ECO:0000313|EMBL:KQR90338.1};
GN   ORFNames=ASG35_00425 {ECO:0000313|EMBL:KQR90338.1};
OS   Burkholderia sp. Leaf177.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR90338.1, ECO:0000313|Proteomes:UP000051826};
RN   [1] {ECO:0000313|EMBL:KQR90338.1, ECO:0000313|Proteomes:UP000051826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf177 {ECO:0000313|EMBL:KQR90338.1,
RC   ECO:0000313|Proteomes:UP000051826};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQR90338.1, ECO:0000313|Proteomes:UP000051826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf177 {ECO:0000313|EMBL:KQR90338.1,
RC   ECO:0000313|Proteomes:UP000051826};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the histone deacetylase family.
CC       {ECO:0000256|ARBA:ARBA00005947}.
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:KQR90338.1}.
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DR   EMBL; LMPF01000001; KQR90338.1; -; Genomic_DNA.
DR   RefSeq; WP_056352814.1; NZ_LMPF01000001.1.
DR   AlphaFoldDB; A0A0Q5PTU1; -.
DR   OrthoDB; 9808367at2; -.
DR   Proteomes; UP000051826; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd10001; HDAC_classII_APAH; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR10625:SF9; HISTONE DEACETYLASE 8; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KQR90338.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051826}.
FT   DOMAIN          32..334
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   340 AA;  37251 MW;  5C05E01E37CDC96C CRC64;
     MQTYFHPSQL KHHPRSYLSR GQMRTPQEIP ERALRLVEAS KNLGFDVREP ADFGSAPLAA
     VHGEKYLRFL EEAHREWKKV PAEWGDEVMS NIYVRENNPL RGVLGQAARY LADGSCPIGA
     DTYESAYWSA QSALAGANAI INGEREAYAL CRPPGHHARA EAAGGFCYLN NAAIAAQALR
     AKYGRVAVLD TDMHHGQGIQ EIFYERGDVL YVSIHGDPTN FYPAVAGFDD ERGTGEGAGY
     NLNLPMPHDS AEEVFFNNLN LAKDALDQFK PDALVLALGF DIYKDDPQAM VAVTTDGFGK
     LGATIGALKL PTLIVQEGGY HIDTLEANAR AFFEGFSSGR
//
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