ID J0LJN7_AURST Unreviewed; 538 AA.
AC J0LJN7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Malate synthase {ECO:0000256|ARBA:ARBA00012636, ECO:0000256|RuleBase:RU000555};
DE EC=2.3.3.9 {ECO:0000256|ARBA:ARBA00012636, ECO:0000256|RuleBase:RU000555};
GN ORFNames=AURDEDRAFT_115689 {ECO:0000313|EMBL:EJD40815.1};
OS Auricularia subglabra (strain TFB-10046 / SS5) (White-rot fungus)
OS (Auricularia delicata (strain TFB10046)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Auriculariaceae; Auricularia.
OX NCBI_TaxID=717982 {ECO:0000313|EMBL:EJD40815.1, ECO:0000313|Proteomes:UP000006514};
RN [1] {ECO:0000313|Proteomes:UP000006514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFB10046 {ECO:0000313|Proteomes:UP000006514};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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 Evidence={ECO:0000256|ARBA:ARBA00001699,
CC ECO:0000256|RuleBase:RU000555};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 2/2. {ECO:0000256|RuleBase:RU000555}.
CC -!- SIMILARITY: Belongs to the malate synthase family.
CC {ECO:0000256|ARBA:ARBA00006394, ECO:0000256|RuleBase:RU000555}.
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DR EMBL; JH687798; EJD40815.1; -; Genomic_DNA.
DR RefSeq; XP_007350980.1; XM_007350918.1.
DR AlphaFoldDB; J0LJN7; -.
DR KEGG; adl:AURDEDRAFT_115689; -.
DR eggNOG; KOG1261; Eukaryota.
DR InParanoid; J0LJN7; -.
DR OMA; WHLPERH; -.
DR OrthoDB; 177378at2759; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000006514; Unassembled WGS sequence.
DR GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniPathway.
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 {ECO:0000256|ARBA:ARBA00022435,
KW ECO:0000256|RuleBase:RU000555};
KW Reference proteome {ECO:0000313|Proteomes:UP000006514};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000555};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU000555}.
FT DOMAIN 4..67
FT /note="Malate synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20656"
FT DOMAIN 157..401
FT /note="Malate synthase TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01274"
FT DOMAIN 407..521
FT /note="Malate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20659"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
FT ACT_SITE 442
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
SQ SEQUENCE 538 AA; 60038 MW; A64F96905D87FAD6 CRC64;
MTVKGVTVLG KRNAQYDEIL TDPALAFLAA LHRTFESTRQ SLLTARIAVQ QRLDAGQYLD
FPSETAHVRA DPSWICAPPA PGLEDRRVEI TGPTDRKMVV NALNSGAKTF MADFEDSNAP
SWANMINGQI NLRDAILRKI DFIQGGKSYK LSKNPAVLLV RPRGWHLDEP RVLVDNRPIS
GGLFDFGLYF FHNAKALVAS GFGPYFYLPK MEHYLEARLW NDVFLFSQSY IHIPHNTIRA
TVLIETLPAA FHMEEILFEL RNHSSGLNCG RWDYIFSFIK KRRADRRAVL PDRKDVTMEV
PFMDAYVRLL IQTCHKRKVA AMGGMSAMIP IKGDEAANEA AMNKVRADKL REVTAGHDGT
WIAHPLINKI AMDIFDKHML GPHQYHVRRE DVKVTAADLL NTSVSGQITE DGVKSNVSAA
LAYSAAWIAG NGCIPLNNLM EDAATAEIAR LQLWQWAHHN AHLDSGDVIT PGYIGKVVDG
VAPNVKSLVA GIKDEHLAIA VSYLKDQVKR PWASDFLTSD LMVYLEKVDG AKWVRSSL
//
