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Database: UniProt
Entry: Q987Q0_RHILO
LinkDB: Q987Q0_RHILO
Original site: Q987Q0_RHILO 
ID   Q987Q0_RHILO            Unreviewed;       346 AA.
AC   Q987Q0;
DT   01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=Acetylpolyamine aminohydrolase {ECO:0000313|EMBL:BAB53153.1};
GN   OrderedLocusNames=mlr6968 {ECO:0000313|EMBL:BAB53153.1};
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB53153.1, ECO:0000313|Proteomes:UP000000552};
RN   [1] {ECO:0000313|EMBL:BAB53153.1, ECO:0000313|Proteomes:UP000000552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC   {ECO:0000313|Proteomes:UP000000552};
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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}.
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DR   EMBL; BA000012; BAB53153.1; -; Genomic_DNA.
DR   RefSeq; WP_010914460.1; NC_002678.2.
DR   AlphaFoldDB; Q987Q0; -.
DR   KEGG; mlo:mlr6968; -.
DR   PATRIC; fig|266835.9.peg.5546; -.
DR   eggNOG; COG0123; Bacteria.
DR   HOGENOM; CLU_007727_8_3_5; -.
DR   Proteomes; UP000000552; Chromosome.
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:BAB53153.1}.
FT   DOMAIN          28..330
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
SQ   SEQUENCE   346 AA;  37748 MW;  C58618029DF8E602 CRC64;
     MKTIFSPIQL KHQGQFEFYN GAVVEGYENT SRATFITSRI EEVRLGPVLN PRPQSLDTAK
     RIHSPTYLDF IASAWRLWRD AGRTGTALPY AWPARGRYKD VAPDSIDAQL GQYSIDASTG
     FVEGTWEAVK ASHDSALTAA DLIIEGEQAC FALCRPPGHH AGTDFNGGYC FVNNAAVAAQ
     RLLDGGASRV TILDIDYHHG NGTQEIFYAR GDVQVVSLHA DPRNDYPFFA GYADERGSGS
     GEGFNINIPL PHGTDWAQWE GALDFALGSV RQFGPDVVVI SHGVDTFEGD PISRFRLSHD
     HFPLIGARLA GLQTKTLFVL EGGYAVEDVG INVVGVLSGY EDAIRR
//
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