SSAT_CRYPI
ID SSAT_CRYPI Reviewed; 152 AA.
AC Q5CPU3;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Diamine acetyltransferase {ECO:0000305|PubMed:17289169};
DE EC=2.3.1.57 {ECO:0000269|PubMed:17289169};
DE AltName: Full=Spermidine/spermine N(1)-acetyltransferase {ECO:0000303|PubMed:17289169};
DE Short=CpSSAT {ECO:0000303|PubMed:17289169};
GN Name=SSAT {ECO:0000303|PubMed:17289169}; ORFNames=cgd4_4000;
OS Cryptosporidium parvum (strain Iowa II).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=353152;
RN [1] {ECO:0000312|EMBL:EAK87438.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa II;
RX PubMed=15044751; DOI=10.1126/science.1094786;
RA Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA Anantharaman V., Aravind L., Kapur V.;
RT "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL Science 304:441-445(2004).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=Iowa II {ECO:0000269|PubMed:17289169};
RX PubMed=17289169; DOI=10.1016/j.molbiopara.2007.01.004;
RA Yarlett N., Wu G., Waters W.R., Harp J.A., Wannemuehler M.J., Morada M.,
RA Athanasopoulos D., Martinez M.P., Upton S.J., Marton L.J., Frydman B.J.;
RT "Cryptosporidium parvum spermidine/spermine N1-acetyltransferase exhibits
RT different characteristics from the host enzyme.";
RL Mol. Biochem. Parasitol. 152:170-180(2007).
CC -!- FUNCTION: Enzyme which catalyzes the acetylation of polyamines.
CC Displays higher substrate specificity for spermine than for spermidine.
CC May function to acetylate host-derived polyamines, thus alleviating the
CC necessity for de novo synthesis of these molecules.
CC {ECO:0000269|PubMed:17289169, ECO:0000303|PubMed:17289169}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an alkane-alpha,omega-diamine = an N-
CC acetylalkane-alpha,omega-diamine + CoA + H(+); Xref=Rhea:RHEA:11116,
CC Rhea:RHEA-COMP:9766, Rhea:RHEA-COMP:9767, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:70977,
CC ChEBI:CHEBI:70988; EC=2.3.1.57;
CC Evidence={ECO:0000269|PubMed:17289169};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 uM for spermine {ECO:0000269|PubMed:17289169};
CC KM=50 uM for spermidine {ECO:0000269|PubMed:17289169};
CC Vmax=79 umol/min/mg enzyme toward spermine
CC {ECO:0000269|PubMed:17289169};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; N-
CC acetylputrescine from putrescine: step 1/1.
CC {ECO:0000305|PubMed:17289169}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17289169}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289169}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000255}.
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DR EMBL; AAEE01000012; EAK87438.1; -; Genomic_DNA.
DR RefSeq; XP_625421.1; XM_625421.1.
DR PDB; 6YUG; X-ray; 1.95 A; A/B=1-152.
DR PDBsum; 6YUG; -.
DR AlphaFoldDB; Q5CPU3; -.
DR SMR; Q5CPU3; -.
DR EnsemblProtists; EAK87438; EAK87438; cgd4_4000.
DR GeneID; 3372423; -.
DR KEGG; cpv:cgd4_4000; -.
DR VEuPathDB; CryptoDB:cgd4_4000; -.
DR InParanoid; Q5CPU3; -.
DR OMA; LECACAG; -.
DR BRENDA; 2.3.1.4; 1728.
DR SABIO-RK; Q5CPU3; -.
DR UniPathway; UPA00188; UER00363.
DR Proteomes; UP000006726; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0004145; F:diamine N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009447; P:putrescine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032918; P:spermidine acetylation; IDA:UniProtKB.
DR GO; GO:0032919; P:spermine acetylation; IDA:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..152
FT /note="Diamine acetyltransferase"
FT /id="PRO_0000430034"
FT DOMAIN 5..152
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT ACT_SITE 127
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A951"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:6YUG"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:6YUG"
FT HELIX 15..22
FT /evidence="ECO:0007829|PDB:6YUG"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:6YUG"
FT HELIX 34..41
FT /evidence="ECO:0007829|PDB:6YUG"
FT STRAND 46..56
FT /evidence="ECO:0007829|PDB:6YUG"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:6YUG"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6YUG"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:6YUG"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:6YUG"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6YUG"
FT HELIX 93..107
FT /evidence="ECO:0007829|PDB:6YUG"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:6YUG"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:6YUG"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:6YUG"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:6YUG"
SQ SEQUENCE 152 AA; 17837 MW; 93DC5867C9B654B2 CRC64;
MISSFEVRKA TIDDYFELRN LICDVTRCTE TLSREQAEER FRYNTYHPYC LVDTENGRIV
GYAGFYIIPH LGRKNDSRIE HVIISKEYRN RGLGRLLCKQ IIEDAKNKFN CGRIDLTVES
HIAKKLYSSL EFEKVNTEVM RNSFLDLTPK SD
