APAH2_PSEAE
ID APAH2_PSEAE Reviewed; 344 AA.
AC Q9I6H0;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Acetylpolyamine amidohydrolase 2 {ECO:0000303|PubMed:26956223};
DE Short=APAH 2 {ECO:0000303|PubMed:26956223};
DE EC=3.5.1.- {ECO:0000269|PubMed:26956223};
DE AltName: Full=Acetylcadaverine deacetylase {ECO:0000305|PubMed:26956223};
DE AltName: Full=Acetylpolyamine deacetylase {ECO:0000305|PubMed:26956223};
DE AltName: Full=Acetylputrescine deacetylase {ECO:0000305|PubMed:26956223};
DE EC=3.5.1.62 {ECO:0000269|PubMed:26956223};
GN Name=aphB {ECO:0000303|PubMed:18192388};
GN OrderedLocusNames=PA0321 {ECO:0000312|EMBL:AAG03710.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., 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.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP INDUCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=18192388; DOI=10.1128/jb.01804-07;
RA Chou H.T., Kwon D.H., Hegazy M., Lu C.D.;
RT "Transcriptome analysis of agmatine and putrescine catabolism in
RT Pseudomonas aeruginosa PAO1.";
RL J. Bacteriol. 190:1966-1975(2008).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=26956223; DOI=10.1186/s12858-016-0063-z;
RA Kraemer A., Herzer J., Overhage J., Meyer-Almes F.J.;
RT "Substrate specificity and function of acetylpolyamine amidohydrolases from
RT Pseudomonas aeruginosa.";
RL BMC Biochem. 17:4-4(2016).
CC -!- FUNCTION: Catalyzes the deacetylation of acetylated polyamines such as
CC N-acetylputrescine and N-acetylcadaverine. Plays an important role in
CC the metabolism of acetylated polyamines in P.aeruginosa. Is involved in
CC the degradation pathways of N-acetylputrescine and N-acetylcadaverine,
CC that allow P.aeruginosa to utilize these acetylpolyamines as a carbon
CC source under glucose starvation. Shows nearly no activity against N(1)-
CC acetylspermine and N(1)-acetylspermidine. Can also hydrolyze artificial
CC trifluoroacetylated lysine-derivative, and to a lesser extent,
CC acetylated lysine-derivative. {ECO:0000269|PubMed:26956223}.
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:0000269|PubMed:26956223};
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:0000269|PubMed:26956223};
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:0000250|UniProtKB:Q48935};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=284 uM for N-acetylcadaverine {ECO:0000269|PubMed:26956223};
CC KM=411 uM for N-acetylputrescine {ECO:0000269|PubMed:26956223};
CC KM=22 uM for Boc-Lys(Ac)-AMC {ECO:0000269|PubMed:26956223};
CC KM=11 uM for Boc-Lys(TFA)-AMC {ECO:0000269|PubMed:26956223};
CC Vmax=7.6 nmol/sec/mg enzyme with N-acetylcadaverine as substrate
CC {ECO:0000269|PubMed:26956223};
CC Vmax=14.2 nmol/sec/mg enzyme with N-acetylputrescine as substrate
CC {ECO:0000269|PubMed:26956223};
CC Vmax=0.017 nmol/sec/mg enzyme with Boc-Lys(Ac)-AMC as substrate
CC {ECO:0000269|PubMed:26956223};
CC Vmax=21 nmol/sec/mg enzyme with Boc-Lys(TFA)-AMC as substrate
CC {ECO:0000269|PubMed:26956223};
CC -!- PATHWAY: Amine and polyamine metabolism. {ECO:0000269|PubMed:26956223}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q48935}.
CC -!- INDUCTION: By exogenous acetylputrescine and agmatine, but not by
CC putrescine. {ECO:0000269|PubMed:18192388}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a markedly delayed
CC growth with a slight hint of increase after 15 hours using N-
CC acetylcadaverine as sole carbon source, and display an elongated lag-
CC phase of approximately 6 hours before growing on N-acetylputrescine.
CC The deletion mutant strain exhibits only marginal changes in biofilm
CC biomass in comparison to the wild-type. {ECO:0000269|PubMed:26956223}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG03710.1; -; Genomic_DNA.
DR PIR; B83605; B83605.
DR RefSeq; NP_249012.1; NC_002516.2.
DR RefSeq; WP_003112950.1; NZ_QZGE01000016.1.
DR AlphaFoldDB; Q9I6H0; -.
DR SMR; Q9I6H0; -.
DR STRING; 287.DR97_3285; -.
DR PaxDb; Q9I6H0; -.
DR DNASU; 878360; -.
DR EnsemblBacteria; AAG03710; AAG03710; PA0321.
DR GeneID; 878360; -.
DR KEGG; pae:PA0321; -.
DR PATRIC; fig|208964.12.peg.337; -.
DR PseudoCAP; PA0321; -.
DR HOGENOM; CLU_007727_8_3_6; -.
DR InParanoid; Q9I6H0; -.
DR OMA; VMEGGYM; -.
DR PhylomeDB; Q9I6H0; -.
DR BioCyc; PAER208964:G1FZ6-324-MON; -.
DR BRENDA; 3.5.1.62; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0047609; F:acetylputrescine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IDA:PseudoCAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006595; P:polyamine metabolic process; IDA:PseudoCAP.
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 Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..344
FT /note="Acetylpolyamine amidohydrolase 2"
FT /id="PRO_0000439408"
FT ACT_SITE 159
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
FT SITE 323
FT /note="Polarizes the scissile carbonyl of the substrate"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
SQ SEQUENCE 344 AA; 37883 MW; 8238194D8911D0CE CRC64;
MLTIYSDDHR LHHGRHELIG GQFTPCFEKP SRADMVLDRV KAVGLGEVRA PRDFGLEPIR
RVHSEGFVRF LQNAWQDWLA TGRSHDMLPI AWPTRRLRQT EPDNIDGRLG YYSFDAGAPI
TAGTWQAITS SANVALSGQS ELANGARSVF SLCRPPGHHA AADYMGGYCF FNNAAIAAQA
FLDRGAGRVA ILDVDYHHGN GTQDIFYDRA DVLFTSIHGD PRFEYPYFLG YADEKGNGVG
TGYNFNYPLA AGSDWATWSQ ALQAAIRQIQ AYAADALIVS LGVDTFKEDP ISQFRLDSPD
YLRMGEAIGK LGLATLFVME GGYAVEEIGI NAVNVLQGFE GVHR
