ID Q9ZRH5_MAIZE Unreviewed; 662 AA.
AC Q9ZRH5;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AAD10504.1};
RN [1] {ECO:0000313|EMBL:AAD10504.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B73 {ECO:0000313|EMBL:AAD10504.1};
RA Miller H.G., Tausta S.L., Rothermel B.A., Steiffel V., Nelson T.M.;
RT "Maize Root and Leaf Isoforms of NADP-dependent Malic Enzyme Are Encoded by
RT Distinct Genes.";
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
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; U39958; AAD10504.1; -; mRNA.
DR AlphaFoldDB; Q9ZRH5; -.
DR SABIO-RK; Q9ZRH5; -.
DR ExpressionAtlas; Q9ZRH5; baseline and differential.
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 CDD; cd05312; NAD_bind_1_malic_enz; 1.
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 2: Evidence at transcript level;
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 188..369
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 379..631
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 211
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 282
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 354
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 355
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 378
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 519
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 562
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 662 AA; 73142 MW; 494AD0D16FE4D165 CRC64;
MISARTAAAS PASLWKQGGR SEGGGSCDGC RTYRNTLRRA AAAKVRALPS RAVEAVKMGS
AAEMEQEEAE VAAAAAGVVV EDHYGEDSAT EELPILPWAF SVARYVSFSW LKKYAEESYF
YISGYTLLRD PHHNKGLAFM EKERDAHHLR GLLPPAVVPQ ELQIKKIMHN LRQYQVPLQR
YMAMMDLQER NERLFYKLLI DNVEELLPVV YTPTVGEACQ KYGSIFRQPQ GLYVSLRDKG
KVLEVLRNWP HRNIQVICVT DGEAILGLGD LGSQGMGIPV GKLALYTALG GVRPSACLPI
TIDVGTNNEK LLNDEFYIGL RQKRATGEEY HELMEEFMAA VKQIYGEKVL IQFEDFANHN
AFNLLAKYSK SHLVFNDDIQ GTASVVLAGL LAALKVVGRT LAEHTYLFLG AGEAGTGIAE
LIALEISKQT SAPIEECRKK IWLVDSKGLI VDSRKNSVQS FKKPWAHEHE PLTTLYDAVQ
SIKPTVLIGT SGVGRTFTKE VVEAMASFNE RPIIFSLSNP TSHSECTAEE AYNWTQVVIF
ASGSPFDPVE YDGKVFVPGQ SNNAYIFPGF GLGLVISGAI RVHEDMLLAA SEALAAQATQ
ENFDKGSIFP PFTNIRKISA RIARAVAAKA YELGLATRLP PPRDLVKYAQ SCMYTPVYRN
YR
//
