ID   MASY_EMENI              Reviewed;         539 AA.
AC   P28344; C8V1E0; Q5AYH7;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 3.
DT   24-JAN-2024, entry version 134.
DE   RecName: Full=Malate synthase, glyoxysomal;
DE            EC=2.3.3.9;
GN   Name=acuE; ORFNames=AN6653;
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=1832736; DOI=10.1007/bf00260638;
RA   Sandeman R.A., Hynes M.J., Fincham J.R.S., Connerton I.F.;
RT   "Molecular organisation of the malate synthase genes of Aspergillus
RT   nidulans and Neurospora crassa.";
RL   Mol. Gen. Genet. 228:445-452(1991).
RN   [2]
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   [3]
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+);
CC         Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288; EC=2.3.3.9;
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC       isocitrate: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Glyoxysome.
CC   -!- SIMILARITY: Belongs to the malate synthase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA39993.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA58182.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X56671; CAA39993.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AACD01000110; EAA58182.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001301; CBF71180.1; -; Genomic_DNA.
DR   PIR; S17773; S17773.
DR   RefSeq; XP_664257.1; XM_659165.1.
DR   AlphaFoldDB; P28344; -.
DR   SMR; P28344; -.
DR   STRING; 227321.P28344; -.
DR   EnsemblFungi; CBF71180; CBF71180; ANIA_06653.
DR   KEGG; ani:AN6653.2; -.
DR   VEuPathDB; FungiDB:AN6653; -.
DR   eggNOG; KOG1261; Eukaryota.
DR   HOGENOM; CLU_018928_3_0_1; -.
DR   InParanoid; P28344; -.
DR   OMA; AGCDSCW; -.
DR   OrthoDB; 177378at2759; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000000560; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005782; C:peroxisomal matrix; IDA:AspGD.
DR   GO; GO:0005777; C:peroxisome; IDA:AspGD.
DR   GO; GO:0004474; F:malate synthase activity; IMP:AspGD.
DR   GO; GO:0045733; P:acetate catabolic process; IMP:AspGD.
DR   GO; GO:0015976; P:carbon utilization; IMP:AspGD.
DR   GO; GO:0009062; P:fatty acid catabolic process; IMP:AspGD.
DR   GO; GO:0006097; P:glyoxylate cycle; IMP:AspGD.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd00727; malate_synt_A; 1.
DR   Gene3D; 3.20.20.360; Malate synthase, domain 3; 1.
DR   Gene3D; 1.20.1220.12; Malate synthase, domain III; 1.
DR   InterPro; IPR044856; Malate_synth_C_sf.
DR   InterPro; IPR011076; Malate_synth_sf.
DR   InterPro; IPR006252; Malate_synthA.
DR   InterPro; IPR019830; Malate_synthase_CS.
DR   InterPro; IPR001465; Malate_synthase_TIM.
DR   InterPro; IPR048355; MS_C.
DR   InterPro; IPR048356; MS_N.
DR   InterPro; IPR046363; MS_N_TIM-barrel_dom.
DR   NCBIfam; TIGR01344; malate_syn_A; 1.
DR   PANTHER; PTHR42902; MALATE SYNTHASE; 1.
DR   PANTHER; PTHR42902:SF1; MALATE SYNTHASE 1-RELATED; 1.
DR   Pfam; PF20659; MS_C; 1.
DR   Pfam; PF20656; MS_N; 1.
DR   Pfam; PF01274; MS_TIM-barrel; 1.
DR   PIRSF; PIRSF001363; Malate_synth; 1.
DR   SUPFAM; SSF51645; Malate synthase G; 1.
DR   PROSITE; PS00510; MALATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Glyoxylate bypass; Glyoxysome; Peroxisome; Reference proteome; Transferase;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..539
FT                   /note="Malate synthase, glyoxysomal"
FT                   /id="PRO_0000166861"
FT   REGION          65..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           537..539
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        449
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        510
FT                   /note="A -> S (in Ref. 1; CAA39993)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   539 AA;  60797 MW;  D29334EA211735F8 CRC64;
     MSQVDAQLKD VAILGSVSNE ARKILTKEAC AFLAILHRTF NPTRKALLQR RVDRQAEIDK
     GHLPDFLPET KHIRDDPSWK GAPPAPGLVD RRVEITGPTD RKMVVNALNS DVWTYMADFE
     DSSAPTWDNM INGQINLYDA IRRQVDFKQG QKEYKLRTDR TLPTLIARAR GWHLDEKHFT
     VDGEPISGSL FDFGLYFFHN AKELVARGFG PYFYLPKMES HLEARLWNDV FNLAQDYIGM
     PRGTIRGTVL IETITAAFEM EEIIYELRDH SSGLNCGRWD YIFSFIKKFR QHPNFVLPDR
     SDVTMTVPFM DAYVKLLIKT CHKRGVHAMG GMAAQIPIKD NAEANDKAME GVRADKLREV
     RAGHDGTWVA HPALASIASE VFNKYMPTPN QMHVRREDVN ITANDLLNTN VPGKITEDGI
     RKNLNIGLSY MEGWLRGVGC IPINYLMEDA ATAEVSRSQL WQWARHGVTT SEGKKVDKAY
     ALRLLKEQAD ALAAKGPKGN KFQLAGRYFA GQVTGEDYAD FLTSLLYNEI SSPGTASKL
//