ACA1_SCHPO
ID ACA1_SCHPO Reviewed; 209 AA.
AC Q09927;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=N-acetyltransferase aca1;
DE EC=2.3.1.271 {ECO:0000250|UniProtKB:E9P8D2};
DE AltName: Full=(S)-1-pyrroline-5-carboxylate acetyltransferase;
DE AltName: Full=L-azetidine-2-carboxylate acetyltransferase;
DE Short=AZC acetyltransferase;
GN Name=aca1 {ECO:0000312|PomBase:SPAC21E11.04};
GN Synonyms=ppr1 {ECO:0000303|PubMed:12761200}; ORFNames=SPAC21E11.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12761200; DOI=10.1093/jb/mvg003;
RA Nomura M., Nakamori S., Takagi H.;
RT "Characterization of novel acetyltransferases found in budding and fission
RT yeasts that detoxify a proline analogue, azetidine-2-carboxylic acid.";
RL J. Biochem. 133:67-74(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: N-acetyltransferase involved in oxidative stress resistance.
CC Acetylates the toxic proline metabolism intermediate (S)-1-pyrroline-5-
CC carboxylate (P5C), or more likely its spontaneously forming tautomer
CC glutamate-5-semialdehyde (GSA) into N-acetyl-GSA for arginine synthesis
CC in the mitochondria. P5C has been shown to increase the levels of
CC reactive oxigen species (ROS) in the cell by inhibiting the function of
CC the respiratory chain in the mitochondria. The enzyme is able to reduce
CC intracellular ROS levels under P5C-induced oxidative stress and
CC protects cells from damage by oxidative stress (By similarity). Also
CC acetylates and thereby detoxifies the proline analog azetidine-2-
CC carboxylate (AZC), however it is unlikely that AZC is a natural
CC substrate as it occurs only in plants belonging to the Lilaceae family
CC (PubMed:12761200). {ECO:0000250|UniProtKB:E9P8D2,
CC ECO:0000269|PubMed:12761200}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-glutamate 5-semialdehyde = CoA + H(+) + N-
CC acetyl-L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:48232,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:58066; EC=2.3.1.271;
CC Evidence={ECO:0000250|UniProtKB:E9P8D2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5-9 for azetidine-2-carboxylate.
CC {ECO:0000269|PubMed:12761200};
CC Temperature dependence:
CC Optimum temperature is 20 degrees Celsius.
CC {ECO:0000269|PubMed:12761200};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12761200}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC Mitochondrion {ECO:0000250|UniProtKB:E9P8D2}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; AB083128; BAB88769.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA91963.1; -; Genomic_DNA.
DR PIR; S62589; S62589.
DR RefSeq; NP_594501.1; NM_001019930.2.
DR AlphaFoldDB; Q09927; -.
DR SMR; Q09927; -.
DR BioGRID; 278449; 31.
DR STRING; 4896.SPAC21E11.04.1; -.
DR MaxQB; Q09927; -.
DR PaxDb; Q09927; -.
DR EnsemblFungi; SPAC21E11.04.1; SPAC21E11.04.1:pep; SPAC21E11.04.
DR GeneID; 2541963; -.
DR KEGG; spo:SPAC21E11.04; -.
DR PomBase; SPAC21E11.04; aca1.
DR VEuPathDB; FungiDB:SPAC21E11.04; -.
DR eggNOG; ENOG502QRFX; Eukaryota.
DR HOGENOM; CLU_013985_42_1_1; -.
DR OMA; PRCSHNC; -.
DR PhylomeDB; Q09927; -.
DR PRO; PR:Q09927; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0046941; F:azetidine-2-carboxylic acid acetyltransferase activity; IDA:PomBase.
DR GO; GO:0006526; P:arginine biosynthetic process; ISO:PomBase.
DR GO; GO:0006562; P:proline catabolic process; ISO:PomBase.
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 Acyltransferase; Cytoplasm; Mitochondrion; Reference proteome; Transferase.
FT CHAIN 1..209
FT /note="N-acetyltransferase aca1"
FT /id="PRO_0000074604"
FT DOMAIN 26..202
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9P8D2"
FT BINDING 128..133
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:E9P8D2"
FT BINDING 155..156
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9P8D2"
SQ SEQUENCE 209 AA; 23809 MW; 06A73775D80946B0 CRC64;
MKDPNTIPPW RCTDFNAWCI AVDKSTNVKN KEELLSTLTY FINYEIEMGQ TYPIDIKMTR
NEAEDFFFKF CTVICVPVES ETSPAPDLAT ASIDWKTSLL GAFYIKPNYP GRCSHICNGG
FLVSPSHRSK GIGRNLANAY LYFAPRIGFK SSVFNLVFAT NIKSIRLWER LNFTRAGIIK
DAGRLKGHEG YVDAYIYQYH FPSLEDALK
