MASY_EMENI
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 25-MAY-2022, entry version 127.
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; 162425.CADANIAP00007436; -.
DR EnsemblFungi; CBF71180; CBF71180; ANIA_06653.
DR EnsemblFungi; EAA58182; EAA58182; AN6653.2.
DR GeneID; 2870422; -.
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; MENVRAD; -.
DR OrthoDB; 358540at2759; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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; 1.20.1220.12; -; 1.
DR Gene3D; 3.20.20.360; -; 1.
DR InterPro; IPR044856; Malate_synth_C_sf.
DR InterPro; IPR011076; Malate_synth_sf.
DR InterPro; IPR006252; Malate_synthA.
DR InterPro; IPR001465; Malate_synthase.
DR InterPro; IPR019830; Malate_synthase_CS.
DR InterPro; IPR046363; MS_N_TIM-barrel_dom.
DR PANTHER; PTHR42902; PTHR42902; 1.
DR Pfam; PF01274; Malate_synthase; 1.
DR PIRSF; PIRSF001363; Malate_synth; 1.
DR SUPFAM; SSF51645; SSF51645; 1.
DR TIGRFAMs; TIGR01344; malate_syn_A; 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