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Database: UniProt
Entry: A0A251USI0_HELAN
LinkDB: A0A251USI0_HELAN
Original site: A0A251USI0_HELAN 
ID   A0A251USI0_HELAN        Unreviewed;       570 AA.
AC   A0A251USI0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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   Name=MASY {ECO:0000313|EMBL:OTG26019.1};
GN   ORFNames=HannXRQ_Chr05g0154041 {ECO:0000313|EMBL:OTG26019.1},
GN   HanXRQr2_Chr05g0228741 {ECO:0000313|EMBL:KAF5807013.1};
OS   Helianthus annuus (Common sunflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG26019.1, ECO:0000313|Proteomes:UP000215914};
RN   [1] {ECO:0000313|EMBL:KAF5807013.1, ECO:0000313|Proteomes:UP000215914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5807013.1};
RX   PubMed=28538728; DOI=10.1038/nature22380;
RA   Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA   Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA   Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA   Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA   Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA   Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA   Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA   Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA   Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA   Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA   Vincourt P., Rieseberg L.H., Langlade N.B.;
RT   "The sunflower genome provides insights into oil metabolism, flowering and
RT   Asterid evolution.";
RL   Nature 546:148-152(2017).
RN   [2] {ECO:0000313|EMBL:OTG26019.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaves {ECO:0000313|EMBL:OTG26019.1};
RA   Langlade N., Munos S.;
RT   "Sunflower complete genome.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAF5807013.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5807013.1};
RA   Gouzy J., Langlade N., Munos S.;
RT   "Helianthus annuus Genome sequencing and assembly Release 2.";
RL   Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00004757,
CC       ECO:0000256|RuleBase:RU000555}.
CC   -!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000256|ARBA:ARBA00004130}.
CC   -!- SIMILARITY: Belongs to the malate synthase family.
CC       {ECO:0000256|ARBA:ARBA00006394, ECO:0000256|RuleBase:RU000555}.
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DR   EMBL; MNCJ02000320; KAF5807013.1; -; Genomic_DNA.
DR   EMBL; CM007894; OTG26019.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A251USI0; -.
DR   STRING; 4232.A0A251USI0; -.
DR   EnsemblPlants; mRNA:HanXRQr2_Chr05g0228741; mRNA:HanXRQr2_Chr05g0228741; HanXRQr2_Chr05g0228741.
DR   Gramene; mRNA:HanXRQr2_Chr05g0228741; mRNA:HanXRQr2_Chr05g0228741; HanXRQr2_Chr05g0228741.
DR   InParanoid; A0A251USI0; -.
DR   OMA; WHLPERH; -.
DR   OrthoDB; 177378at2759; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000215914; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004474; F:malate synthase activity; IBA:GO_Central.
DR   GO; GO:0006097; P:glyoxylate cycle; IBA:GO_Central.
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   Acyltransferase {ECO:0000313|EMBL:KAF5807013.1};
KW   Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435,
KW   ECO:0000256|RuleBase:RU000555}; Glyoxysome {ECO:0000256|ARBA:ARBA00022453};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215914};
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          27..90
FT                   /note="Malate synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20656"
FT   DOMAIN          181..432
FT                   /note="Malate synthase TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01274"
FT   DOMAIN          437..559
FT                   /note="Malate synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20659"
FT   ACT_SITE        185
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
FT   ACT_SITE        471
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
SQ   SEQUENCE   570 AA;  64508 MW;  FFB419F4BB9152A3 CRC64;
     MSSSLGYYGD TAMKKIPGGV GGYDVPNGVD IRGRYDEEFA KILTKDALIF VAELQREFRS
     HVKYAMECRK EAKMRYNSGG LPGFDPATRH VREGDWVCAE VPPAVADRRV EITGPVERKM
     IINALNSGAK VFMADFEDAL SPTWENLMRG QVNLKDAVNG TISFQDKARN RVYKLNDQTA
     KLFVRPRGWH LPESHIFIDG EPAIGCLVDF GLYFHHNHAP FRKTQGQGYG PFFYLPKMEN
     SREARIWNNV FERAENMAGI EKGSIRATVL IETLPAVFQM DEILYELRDH SVGLNCGRWD
     YIFSYVKTFQ AHPDRLLPDR VLVGMGQHFM RSYSDLLIRT CHRRGVHAMG GMAAQIPIRD
     DPAANEAALE LVKKDKLREV RAGHDGTWAA HPGLIPPIME VFNNNMDDKP NLIKTMKRED
     AANITEEDLL QIPRGVRTME GLRLNTRVGI QYLAAWLTGT GSVPLYNLME DAATAEISRV
     QNWQWLKYGV ELDGDGLGVR VSTELFGKVV EEEMARIERE VGSERFKKGM YKEACKIFTR
     QCTAPVLDDF LTLNAYNHIV VHHPRGPSKL
//
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