APAHL_BURP1
ID APAHL_BURP1 Reviewed; 341 AA.
AC Q3JUN4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Acetylpolyamine amidohydrolase {ECO:0000250|UniProtKB:Q48935};
DE Short=APAH {ECO:0000250|UniProtKB:Q48935};
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q48935};
DE AltName: Full=Acetylcadaverine deacetylase {ECO:0000250|UniProtKB:Q48935};
DE AltName: Full=Acetylpolyamine deacetylase {ECO:0000250|UniProtKB:Q48935};
DE AltName: Full=Acetylputrescine deacetylase {ECO:0000250|UniProtKB:Q48935};
DE EC=3.5.1.62 {ECO:0000250|UniProtKB:Q48935};
GN Name=aphA {ECO:0000312|EMBL:ABA50461.1}; OrderedLocusNames=BURPS1710b_1309;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ZINC, COFACTOR, AND
RP SUBUNIT.
RX PubMed=21359836; DOI=10.1007/s10969-011-9101-7;
RA Abendroth J., Gardberg A.S., Robinson J.I., Christensen J.S., Staker B.L.,
RA Myler P.J., Stewart L.J., Edwards T.E.;
RT "SAD phasing using iodide ions in a high-throughput structural genomics
RT environment.";
RL J. Struct. Funct. Genomics 12:83-95(2011).
CC -!- FUNCTION: Involved in polyamine metabolism. Catalyzes the deacetylation
CC of various acetylated polyamines such as N-acetylputrescine and N-
CC acetylcadaverine. {ECO:0000250|UniProtKB:Q48935}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetylputrescine = acetate + putrescine;
CC Xref=Rhea:RHEA:23412, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:58263, ChEBI:CHEBI:326268; EC=3.5.1.62;
CC Evidence={ECO:0000250|UniProtKB:Q48935};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetylcadaverine = acetate + cadaverine;
CC Xref=Rhea:RHEA:51892, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:58384, ChEBI:CHEBI:134408;
CC Evidence={ECO:0000250|UniProtKB:Q48935};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q48935};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:21359836};
CC -!- PATHWAY: Amine and polyamine metabolism.
CC {ECO:0000250|UniProtKB:Q48935}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:21359836}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. {ECO:0000305}.
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DR EMBL; CP000124; ABA50461.1; -; Genomic_DNA.
DR RefSeq; WP_004526398.1; NC_007434.1.
DR PDB; 3MEN; X-ray; 2.20 A; A/B/C/D=1-341.
DR PDBsum; 3MEN; -.
DR AlphaFoldDB; Q3JUN4; -.
DR SMR; Q3JUN4; -.
DR EnsemblBacteria; ABA50461; ABA50461; BURPS1710b_1309.
DR KEGG; bpm:BURPS1710b_1309; -.
DR HOGENOM; CLU_007727_8_3_4; -.
DR OMA; VMEGGYM; -.
DR OrthoDB; 1443295at2; -.
DR EvolutionaryTrace; Q3JUN4; -.
DR Proteomes; UP000002700; Chromosome I.
DR GO; GO:0047609; F:acetylputrescine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.800.20; -; 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 Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; SSF52768; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..341
FT /note="Acetylpolyamine amidohydrolase"
FT /id="PRO_0000411983"
FT ACT_SITE 157
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:21359836,
FT ECO:0007744|PDB:3MEN"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:21359836,
FT ECO:0007744|PDB:3MEN"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:21359836,
FT ECO:0007744|PDB:3MEN"
FT SITE 320
FT /note="Polarizes the scissile carbonyl of the substrate"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:3MEN"
FT HELIX 7..11
FT /evidence="ECO:0007829|PDB:3MEN"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:3MEN"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:3MEN"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:3MEN"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:3MEN"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:3MEN"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3MEN"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3MEN"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:3MEN"
FT HELIX 122..141
FT /evidence="ECO:0007829|PDB:3MEN"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:3MEN"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3MEN"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:3MEN"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:3MEN"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:3MEN"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:3MEN"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:3MEN"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:3MEN"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:3MEN"
FT STRAND 207..216
FT /evidence="ECO:0007829|PDB:3MEN"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:3MEN"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:3MEN"
FT HELIX 252..269
FT /evidence="ECO:0007829|PDB:3MEN"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:3MEN"
FT HELIX 295..306
FT /evidence="ECO:0007829|PDB:3MEN"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:3MEN"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:3MEN"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:3MEN"
SQ SEQUENCE 341 AA; 37387 MW; 872AC72DB0163811 CRC64;
MLTYFHPDQS LHHPRTYFSR GRMRMPQEVP ERAARLVAAA FAMGFPVREP DDFGIAPIAA
VHDTHYLRFL ETVHREWKAM PEDWGDEAMS NIFVREPNAL RGVLAQAARH LADGSCPVGE
HTWRAAYWSA QSALAAAAAV RDGAPAAYAL CRPPGHHARV DAAGGFCYLN NAAIAAQALR
ARHARVAVLD TDMHHGQGIQ EIFYARRDVL YVSIHGDPTN FYPAVAGFDD ERGAGEGLGY
NVNLPMPHGS SEAAFFERVD DALRELRRFA PDALVLSLGF DVYRDDPQSQ VAVTTDGFGR
LGHLIGALRL PTVIVQEGGY HIESLEANAR SFFGGFGALR G
