APAH1_PSEAE
ID APAH1_PSEAE Reviewed; 346 AA.
AC Q9I3T5;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Acetylpolyamine amidohydrolase 1 {ECO:0000303|PubMed:26956223};
DE Short=APAH 1 {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:18192388, ECO:0000305|PubMed:26956223};
DE EC=3.5.1.62 {ECO:0000269|PubMed:18192388, ECO:0000269|PubMed:26956223};
GN Name=aphA {ECO:0000303|PubMed:18192388, ECO:0000312|EMBL:AAG04798.1};
GN OrderedLocusNames=PA1409 {ECO:0000312|EMBL:AAG04798.1};
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 CATALYTIC ACTIVITY, AND 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, N-acetylcadaverine, N(1)-acetylspermine and N(1)-
CC acetylspermidine. Plays an important role in the metabolism of
CC acetylated polyamines in P.aeruginosa. Is involved in the degradation
CC pathways of N-acetylputrescine and N-acetylcadaverine, that allow
CC P.aeruginosa to utilize these acetylpolyamines as a carbon source under
CC glucose starvation. In vitro, can also hydrolyze artificial
CC trifluoroacetylated and acetylated lysine-derivatives.
CC {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:18192388, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1)-acetylspermine = acetate + spermine;
CC Xref=Rhea:RHEA:51896, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:45725, ChEBI:CHEBI:58101;
CC Evidence={ECO:0000269|PubMed:26956223};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1)-acetylspermidine = acetate + spermidine;
CC Xref=Rhea:RHEA:51900, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:58324;
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=465 uM for N-acetylcadaverine {ECO:0000269|PubMed:26956223};
CC KM=503 uM for N-acetylputrescine {ECO:0000269|PubMed:26956223};
CC KM=223 uM for Boc-Lys(Ac)-AMC {ECO:0000269|PubMed:26956223};
CC KM=84 uM for Boc-Lys(TFA)-AMC {ECO:0000269|PubMed:26956223};
CC Vmax=24.5 nmol/sec/mg enzyme with N-acetylcadaverine as substrate
CC {ECO:0000269|PubMed:26956223};
CC Vmax=39.3 nmol/sec/mg enzyme with N-acetylputrescine as substrate
CC {ECO:0000269|PubMed:26956223};
CC Vmax=1.3 nmol/sec/mg enzyme with Boc-Lys(Ac)-AMC as substrate
CC {ECO:0000269|PubMed:26956223};
CC Vmax=5.2 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 are unable to use N-
CC acetylcadaverine as sole carbon source for growth, and display an
CC elongated lag-phase of approximately 6 hours before growing on N-
CC acetylputrescine. The deletion mutant strain exhibits only marginal
CC changes in biofilm biomass in comparison to the wild-type.
CC {ECO:0000269|PubMed:26956223}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG04798.1; -; Genomic_DNA.
DR PIR; H83469; H83469.
DR RefSeq; NP_250100.1; NC_002516.2.
DR RefSeq; WP_003112424.1; NZ_QZGE01000005.1.
DR AlphaFoldDB; Q9I3T5; -.
DR SMR; Q9I3T5; -.
DR STRING; 287.DR97_614; -.
DR PaxDb; Q9I3T5; -.
DR PRIDE; Q9I3T5; -.
DR DNASU; 879295; -.
DR EnsemblBacteria; AAG04798; AAG04798; PA1409.
DR GeneID; 879295; -.
DR KEGG; pae:PA1409; -.
DR PATRIC; fig|208964.12.peg.1458; -.
DR PseudoCAP; PA1409; -.
DR HOGENOM; CLU_007727_8_3_6; -.
DR InParanoid; Q9I3T5; -.
DR OMA; FRAEWIL; -.
DR PhylomeDB; Q9I3T5; -.
DR BioCyc; PAER208964:G1FZ6-1435-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..346
FT /note="Acetylpolyamine amidohydrolase 1"
FT /id="PRO_0000439407"
FT ACT_SITE 161
FT /note="Proton donor/acceptor"
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 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
FT SITE 325
FT /note="Polarizes the scissile carbonyl of the substrate"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
SQ SEQUENCE 346 AA; 37954 MW; D5265B16D42D04BA CRC64;
MLSVYSDDHR LHFGQSELVD GKLQPCFEMP SRADTVLARV KSQNLGEVIA PKDFGREPLL
RLHDAAYLDF LQGAWARWTA EGHSGDLVST TFPGRRLRRD GPIPTALMGE LGYYSFDTEA
PITAGTWQAI YSSAQVALTA QEHMRQGARS AFALCRPPGH HAGGDFMGGY CFLNNAAIAT
QAFLDQGARR VAILDVDYHH GNGTQDIFYR RDDVLFASIH GDPRVEYPYF LGYADERGEG
AGEGCNHNYP LAHGSGWDLW SAALDDACVR IAGYAPDALV ISLGVDTYKE DPISQFRLDS
PDYLRMGERI ARLGLPTLFI MEGGYAVEAI GINAVNVLQG YEGAAR
