AATA_EMENI
ID AATA_EMENI Reviewed; 357 AA.
AC P21133; C8VHS6; Q5BA07;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase 40 kDa form {ECO:0000303|PubMed:2120195};
DE EC=2.3.1.164 {ECO:0000269|PubMed:2110531, ECO:0000269|PubMed:2120195};
DE AltName: Full=Isopenicillin-N N-acyltransferase {ECO:0000303|PubMed:2120195};
DE Contains:
DE RecName: Full=Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase 11 kDa subunit {ECO:0000250|UniProtKB:P15802};
DE Contains:
DE RecName: Full=Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase 29 kDa subunit {ECO:0000250|UniProtKB:P15802};
GN Name=penDE {ECO:0000303|PubMed:2120195}; Synonyms=aat; ORFNames=AN2623;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2166227; DOI=10.1007/bf00259395;
RA Montenegro E., Barredo J.L., Gutierrez S., Diez B., Alvarez E.,
RA Martin J.F.;
RT "Cloning, characterization of the acyl-CoA:6-amino penicillanic acid
RT acyltransferase gene of Aspergillus nidulans and linkage to the
RT isopenicillin N synthase gene.";
RL Mol. Gen. Genet. 221:322-330(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, CATALYTIC ACTIVITY,
RP AND PATHWAY.
RX PubMed=2120195; DOI=10.1128/jb.172.10.5908-5914.1990;
RA Tobin M.B., Fleming M.D., Skatrud P.L., Miller J.R.;
RT "Molecular characterization of the acyl-coenzyme A:isopenicillin N
RT acyltransferase gene (penDE) from Penicillium chrysogenum and Aspergillus
RT nidulans and activity of recombinant enzyme in Escherichia coli.";
RL J. Bacteriol. 172:5908-5914(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [5]
RP PROTEIN SEQUENCE OF 103-122, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=2110531; DOI=10.1016/0014-5793(90)80224-7;
RA Whiteman P.A., Abraham E.P., Baldwin J.E., Fleming M.D., Schofield C.J.,
RA Sutherland J.D., Willis A.C.;
RT "Acyl coenzyme A: 6-aminopenicillanic acid acyltransferase from Penicillium
RT chrysogenum and Aspergillus nidulans.";
RL FEBS Lett. 262:342-344(1990).
CC -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC that mediates the biosynthesis of penicillin, the world's most
CC important antibiotic (PubMed:2120195, PubMed:2110531). AatA catalyzes
CC the exchange of the alpha-aminoadipyl side chain of isopenicillin N for
CC phenylacetic acid to yield penicillin (PubMed:2120195, PubMed:2110531).
CC This step occurs in the peroxisomal matrix and the penM and paaT
CC transporters are involved in the isopenicillin N and phenylacetic acid
CC import into the peroxisome, respectively (By similarity). The
CC penicillin biosynthesis occurs via 3 enzymatic steps, the first
CC corresponding to the production of the tripeptide N-[(5S)-5-amino-5-
CC carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) by the NRPS
CC acvA. The tripeptide ACV is then cyclized to isopenicillin N (IPN) by
CC the isopenicillin N synthase ipnA that forms the beta-lactam nucleus.
CC Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic
CC acid by the isopenicillin N acyltransferase penDE to yield penicillin
CC in the peroxisomal matrix (By similarity).
CC {ECO:0000250|UniProtKB:P15802, ECO:0000269|PubMed:2110531,
CC ECO:0000269|PubMed:2120195}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + isopenicillin N + phenylacetyl-CoA = CoA + H(+) + L-2-
CC aminoadipate + penicillin G; Xref=Rhea:RHEA:20720, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:51354, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57390, ChEBI:CHEBI:58399, ChEBI:CHEBI:58672;
CC EC=2.3.1.164; Evidence={ECO:0000269|PubMed:2110531,
CC ECO:0000269|PubMed:2120195};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20721;
CC Evidence={ECO:0000269|PubMed:2110531, ECO:0000269|PubMed:2120195};
CC -!- PATHWAY: Antibiotic biosynthesis; penicillin G biosynthesis; penicillin
CC G from L-alpha-aminoadipate and L-cysteine and L-valine: step 3/3.
CC {ECO:0000269|PubMed:2110531, ECO:0000269|PubMed:2120195}.
CC -!- SUBUNIT: The active form of the enzyme results from processing of the
CC 40-kDa monomeric precursor to a heterodimer containing subunits of 11
CC and 29 kDa. {ECO:0000269|PubMed:2110531, ECO:0000269|PubMed:2120195}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:P15802}.
CC Note=The unprocessed preprotein is translocated inside peroxisomes and
CC regulates its self-processing. {ECO:0000250|UniProtKB:P15802}.
CC -!- PTM: The pre-AAT protein is synthesized as 40 kDa precursor which is
CC then self-processed into an 11 kDa (protein A) and a 29 kDa (protein
CC B). The B protein carries AAT activity. {ECO:0000269|PubMed:2120195}.
CC -!- SIMILARITY: Belongs to the peptidase C45 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA62970.1; Type=Erroneous gene model prediction; Evidence={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; X53310; CAA37394.1; -; Genomic_DNA.
DR EMBL; M58293; AAA33287.1; -; Genomic_DNA.
DR EMBL; AACD01000045; EAA62970.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001306; CBF84346.1; -; Genomic_DNA.
DR PIR; S12169; S12169.
DR RefSeq; XP_660227.1; XM_655135.1.
DR AlphaFoldDB; P21133; -.
DR SMR; P21133; -.
DR STRING; 162425.CADANIAP00010503; -.
DR MEROPS; C45.001; -.
DR EnsemblFungi; CBF84346; CBF84346; ANIA_02623.
DR EnsemblFungi; EAA62970; EAA62970; AN2623.2.
DR GeneID; 2874539; -.
DR KEGG; ani:AN2623.2; -.
DR VEuPathDB; FungiDB:AN2623; -.
DR eggNOG; ENOG502RY9N; Eukaryota.
DR HOGENOM; CLU_037787_1_0_1; -.
DR InParanoid; P21133; -.
DR OMA; NWDFFSA; -.
DR OrthoDB; 872824at2759; -.
DR BioCyc; MetaCyc:MON-19537; -.
DR BioCyc; MetaCyc:MON-19538; -.
DR UniPathway; UPA00149; UER00241.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005782; C:peroxisomal matrix; ISS:GO_Central.
DR GO; GO:0102920; F:acyl coenzyme A: isopenicillin N acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0050640; F:isopenicillin-N N-acyltransferase activity; IMP:AspGD.
DR GO; GO:0042318; P:penicillin biosynthetic process; IMP:AspGD.
DR InterPro; IPR005079; Peptidase_C45.
DR Pfam; PF03417; AAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Antibiotic biosynthesis; Direct protein sequencing;
KW Peroxisome; Reference proteome; Transferase; Zymogen.
FT CHAIN 1..357
FT /note="Acyl-coenzyme A:6-aminopenicillanic-acid-
FT acyltransferase 40 kDa form"
FT /id="PRO_0000020592"
FT CHAIN 1..102
FT /note="Acyl-coenzyme A:6-aminopenicillanic-acid-
FT acyltransferase 11 kDa subunit"
FT /id="PRO_0000020593"
FT CHAIN 103..357
FT /note="Acyl-coenzyme A:6-aminopenicillanic-acid-
FT acyltransferase 29 kDa subunit"
FT /id="PRO_0000020594"
FT BINDING 121
FT /ligand="6-aminopenicillanate"
FT /ligand_id="ChEBI:CHEBI:57869"
FT /evidence="ECO:0000250|UniProtKB:P15802"
FT BINDING 310
FT /ligand="6-aminopenicillanate"
FT /ligand_id="ChEBI:CHEBI:57869"
FT /evidence="ECO:0000250|UniProtKB:P15802"
SQ SEQUENCE 357 AA; 39236 MW; 89129F003CA0A00C CRC64;
MLHVTCQGTP SEIGYHHGSA AKGEIAKAID FATGLIHGKT KKTQAELEQL LRELEQVMKQ
RWPRYYEEIC GIAKGAEREV SEIVMLNTRT EFAYGLVEAR DGCTTVYCKT PNGALQGQNW
DFFTATKENL IQLTICQPGL PTIKMITEAG IIGKVGFNSA GVAVNYNALH LHGLRPTGLP
SHLALRMALE STSPSEAYEK IVSQGGMAAS AFIMVGNAHE AYGLEFSPIS LCKQVADTNG
RIVHTNHCLL NHGPSAQELN PLPDSWSRHG RMEHLLSGFD GTKEAFAKLW EDEDNYPLSI
CRAYKEGKSR GSTLFNIVFD HVGRKATVRL GRPNNPDETF VMTFSNLDTK SAIQANI
