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Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase 40 kDa form (EC 2.3.1.164) (Isopenicillin-N N-acyltransferase) [Cleaved into: Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase 11 kDa subunit; Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase 29 kDa subunit]

 AAAA_PENCH              Reviewed;         357 AA.
P15802;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
05-DEC-2018, entry version 85.
RecName: Full=Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase 40 kDa form;
EC=2.3.1.164;
AltName: Full=Isopenicillin-N N-acyltransferase;
Contains:
RecName: Full=Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase 11 kDa subunit;
Contains:
RecName: Full=Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase 29 kDa subunit;
Name=penDE; Synonyms=aat;
Penicillium chrysogenum (Penicillium notatum).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
Penicillium chrysogenum species complex.
NCBI_TaxID=5076;
[1]
NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 1-31 AND 104-129.
STRAIN=AS-P-78;
PubMed=2555269; DOI=10.1016/0378-1119(89)90115-7;
Barredo J.L., van Solingen P., Diez B., Alvarez E., Cantoral J.M.,
Kattevilder A., Smaal E.B., Groenen M.A.M., Veenstra A.E.,
Martin J.F.;
"Cloning and characterization of the acyl-coenzyme A: 6-
aminopenicillanic-acid-acyltransferase gene of Penicillium
chrysogenum.";
Gene 83:291-300(1989).
[2]
NUCLEOTIDE SEQUENCE.
PubMed=2120195; DOI=10.1128/jb.172.10.5908-5914.1990;
Tobin M.B., Fleming M.D., Skatrud P.L., Miller J.R.;
"Molecular characterization of the acyl-coenzyme A:isopenicillin N
acyltransferase gene (penDE) from Penicillium chrysogenum and
Aspergillus nidulans and activity of recombinant enzyme in Escherichia
coli.";
J. Bacteriol. 172:5908-5914(1990).
[3]
PROTEIN SEQUENCE OF 1-20; 103-131; 188-200; 258-265 AND 316-323.
PubMed=2110531; DOI=10.1016/0014-5793(90)80224-7;
Whiteman P.A., Abraham E.P., Baldwin J.E., Fleming M.D.,
Schofield C.J., Sutherland J.D., Willis A.C.;
"Acyl coenzyme A: 6-aminopenicillanic acid acyltransferase from
Penicillium chrysogenum and Aspergillus nidulans.";
FEBS Lett. 262:342-344(1990).
[4]
CHARACTERIZATION.
PubMed=8396910; DOI=10.1042/bj2940357;
Aplin R.T., Baldwin J.E., Roach P.L., Robinson C.V., Schofield C.J.;
"Investigations into the post-translational modification and mechanism
of isopenicillin N:acyl-CoA acyltransferase using electrospray mass
spectrometry.";
Biochem. J. 294:357-363(1993).
-!- FUNCTION: Last enzyme in penicillin biosynthetic pathway, which
converts isopenicillin N (IPN) to penicillin G, using phenyl-
acetyl-CoA or phenoxyacetyl-CoA as acyl donors.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + isopenicillin N + phenylacetyl-CoA = CoA + H(+) +
L-2-aminoadipate + penicillin G; Xref=Rhea:RHEA:20720,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:51354,
ChEBI:CHEBI:57287, ChEBI:CHEBI:57390, ChEBI:CHEBI:58399,
ChEBI:CHEBI:58672; EC=2.3.1.164;
-!- PATHWAY: Antibiotic biosynthesis; penicillin G biosynthesis;
penicillin G from L-alpha-aminoadipate and L-cysteine and L-
valine: step 3/3.
-!- MISCELLANEOUS: The pre-AAT protein is probably synthesized as 40
kDa precursor which is then processed into an 11 kDa (protein A)
and a 29 kDa (protein B). The B protein carries AAT activity.
-!- SIMILARITY: Belongs to the peptidase C45 family. {ECO:0000305}.
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EMBL; M31454; AAA33692.1; -; Genomic_DNA.
EMBL; A15528; CAA01234.1; -; Unassigned_DNA.
EMBL; A15359; CAA01221.1; -; Unassigned_DNA.
PIR; JQ0118; JQ0118.
PDB; 2X1C; X-ray; 1.85 A; A/B/C/D=1-357.
PDB; 2X1D; X-ray; 1.64 A; A/B/C/D=1-357.
PDB; 2X1E; X-ray; 2.00 A; A/B/C/D=1-357.
PDBsum; 2X1C; -.
PDBsum; 2X1D; -.
PDBsum; 2X1E; -.
SMR; P15802; -.
MEROPS; C45.001; -.
eggNOG; ENOG410JNG2; Eukaryota.
eggNOG; ENOG410XSKX; LUCA.
PhylomeDB; P15802; -.
BioCyc; MetaCyc:MONOMER-13369; -.
BRENDA; 2.3.1.164; 4606.
UniPathway; UPA00149; UER00241.
EvolutionaryTrace; P15802; -.
PMAP-CutDB; P15802; -.
GO; GO:0102920; F:acyl coenzyme A: isopenicillin N acyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0050640; F:isopenicillin-N N-acyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
InterPro; IPR005079; Peptidase_C45.
Pfam; PF03417; AAT; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Antibiotic biosynthesis;
Direct protein sequencing; Transferase; Zymogen.
CHAIN 1 357 Acyl-coenzyme A:6-aminopenicillanic-acid-
acyltransferase 40 kDa form.
/FTId=PRO_0000020595.
CHAIN 1 102 Acyl-coenzyme A:6-aminopenicillanic-acid-
acyltransferase 11 kDa subunit.
/FTId=PRO_0000020596.
CHAIN 103 357 Acyl-coenzyme A:6-aminopenicillanic-acid-
acyltransferase 29 kDa subunit.
/FTId=PRO_0000020597.
CONFLICT 103 103 C -> W (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 125 125 A -> P (in Ref. 3; AA sequence).
{ECO:0000305}.
STRAND 3 9 {ECO:0000244|PDB:2X1D}.
HELIX 10 20 {ECO:0000244|PDB:2X1D}.
HELIX 22 37 {ECO:0000244|PDB:2X1D}.
HELIX 44 61 {ECO:0000244|PDB:2X1D}.
HELIX 63 76 {ECO:0000244|PDB:2X1D}.
HELIX 80 87 {ECO:0000244|PDB:2X1D}.
HELIX 89 100 {ECO:0000244|PDB:2X1D}.
STRAND 104 108 {ECO:0000244|PDB:2X1D}.
STRAND 115 122 {ECO:0000244|PDB:2X1D}.
HELIX 124 129 {ECO:0000244|PDB:2X1D}.
STRAND 130 136 {ECO:0000244|PDB:2X1D}.
STRAND 143 148 {ECO:0000244|PDB:2X1D}.
STRAND 155 158 {ECO:0000244|PDB:2X1D}.
STRAND 163 167 {ECO:0000244|PDB:2X1D}.
HELIX 181 189 {ECO:0000244|PDB:2X1D}.
HELIX 194 203 {ECO:0000244|PDB:2X1D}.
STRAND 206 209 {ECO:0000244|PDB:2X1D}.
STRAND 211 216 {ECO:0000244|PDB:2X1D}.
STRAND 221 227 {ECO:0000244|PDB:2X1D}.
STRAND 230 234 {ECO:0000244|PDB:2X1D}.
STRAND 240 244 {ECO:0000244|PDB:2X1D}.
HELIX 263 277 {ECO:0000244|PDB:2X1D}.
HELIX 283 289 {ECO:0000244|PDB:2X1D}.
TURN 294 297 {ECO:0000244|PDB:2X1D}.
STRAND 298 301 {ECO:0000244|PDB:2X1D}.
TURN 306 308 {ECO:0000244|PDB:2X1D}.
STRAND 312 320 {ECO:0000244|PDB:2X1D}.
TURN 321 324 {ECO:0000244|PDB:2X1D}.
STRAND 325 331 {ECO:0000244|PDB:2X1D}.
STRAND 337 343 {ECO:0000244|PDB:2X1D}.
HELIX 346 353 {ECO:0000244|PDB:2X1D}.
SEQUENCE 357 AA; 39939 MW; 7A05822312D1CF08 CRC64;
MLHILCQGTP FEIGYEHGSA AKAVIARSID FAVDLIRGKT KKTDEELKQV LSQLGRVIEE
RWPKYYEEIR GIAKGAERDV SEIVMLNTRT EFAYGLKAAR DGCTTAYCQL PNGALQGQNW
DFFSATKENL IRLTIRQAGL PTIKFITEAG IIGKVGFNSA GVAVNYNALH LQGLRPTGVP
SHIALRIALE STSPSQAYDR IVEQGGMAAS AFIMVGNGHE AFGLEFSPTS IRKQVLDANG
RMVHTNHCLL QHGKNEKELD PLPDSWNRHQ RMEFLLDGFD GTKQAFAQLW ADEDNYPFSI
CRAYEEGKSR GATLFNIIYD HARREATVRL GRPTNPDEMF VMRFDEEDER SALNARL


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