ID C8ZJZ8_9POAL Unreviewed; 365 AA.
AC C8ZJZ8;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
DE Flags: Fragment;
GN Name=nadpme-IV {ECO:0000313|EMBL:CAZ48515.1};
OS Spinifex littoreus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Spinifex.
OX NCBI_TaxID=435770 {ECO:0000313|EMBL:CAZ48515.1};
RN [1] {ECO:0000313|EMBL:CAZ48515.1}
RP NUCLEOTIDE SEQUENCE.
RA Christin P.A., Samaritani E., Petitpierre B., Salamin N., Besnard G.;
RT "Evolutionary Insights on C4 Photosynthetic Subtypes in Grasses from
RT Genomics and Phylogenetics.";
RL Genome Biol. Evol. 1:221-230(2009).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|PIRSR:PIRSR000106-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003426}.
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DR EMBL; FN397738; CAZ48515.1; -; Genomic_DNA.
DR AlphaFoldDB; C8ZJZ8; -.
DR GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006108; P:malate metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR015884; Malic_enzyme_CS.
DR InterPro; IPR012301; Malic_N_dom.
DR InterPro; IPR037062; Malic_N_dom_sf.
DR InterPro; IPR012302; Malic_NAD-bd.
DR InterPro; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF92; NADP-DEPENDENT MALIC ENZYME, CHLOROPLASTIC; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000106-3}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003426}.
FT DOMAIN 1..172
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 182..365
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 14
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 85
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 157
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 158
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 181
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAZ48515.1"
FT NON_TER 365
FT /evidence="ECO:0000313|EMBL:CAZ48515.1"
SQ SEQUENCE 365 AA; 39719 MW; EFCA3175965B1441 CRC64;
LLIDNVEELL PFVYTPTVGE ACQKYGSIFR QPQGLYVSLR DKGRVLEVLR NWPQRDIQVI
CVTDGGRILG LGDLGAQGMG IPVGKLALYT ALGGVRPSAC LPITIDVGTN NEALLNDEFY
IGLRQKRATG KEYHELIEEF MSAVVQIYGE KVLIQFEDFA NHNAFDLLEK YSKSHLVFND
DIQGTASVVL AGLLASLKVV GGTLAEHTYL FLGAGEAGTG IAELIALQIS KQTKAPIEEC
RQKVWLVDSK GLIVSSRKDS LPSFKKPWAH EHEPVATLFD AVQSIKPTVL IGTSGVGRAF
TKEVVEAMAS FNERPVIFSL SNPTSCSECT AEQAYTWTKG RAVFASGSPF SPVEYEGKTF
VPGQA
//
