ID A0A1W4WUV5_AGRPL Unreviewed; 630 AA.
AC A0A1W4WUV5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=NADP-dependent malic enzyme-like isoform X2 {ECO:0000313|RefSeq:XP_018327664.1};
GN Name=LOC108738647 {ECO:0000313|RefSeq:XP_018327664.1};
OS Agrilus planipennis (Emerald ash borer) (Agrilus marcopoli).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia;
OC Buprestoidea; Buprestidae; Agrilinae; Agrilus.
OX NCBI_TaxID=224129 {ECO:0000313|Proteomes:UP000192223, ECO:0000313|RefSeq:XP_018327664.1};
RN [1] {ECO:0000313|RefSeq:XP_018327664.1}
RP IDENTIFICATION.
RC TISSUE=Entire body {ECO:0000313|RefSeq:XP_018327664.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785}.
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DR RefSeq; XP_018327664.1; XM_018472162.2.
DR AlphaFoldDB; A0A1W4WUV5; -.
DR EnsemblMetazoa; XM_018472162.2; XP_018327664.1; LOC108738647.
DR GeneID; 108738647; -.
DR OrthoDB; 1069499at2759; -.
DR Proteomes; UP000192223; Unplaced.
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 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; 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:SF90; MALIC ENZYME-RELATED; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000192223}.
FT DOMAIN 127..308
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 318..571
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 150
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 221
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 293
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 294
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 317
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 458
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 502
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 630 AA; 69727 MW; 0BBBEE0F3063FD18 CRC64;
MLPAVSRSLL SNGPTSRIVL TSCRHGIIGV APCNNSTSFE NGLQRCKFHS VGGKIISPSQ
VKGIDHLRDP RLNKGLAFTL EERQLLGIHG LQPPRFKTQE EQIEICQESV RRYNDDLNKY
LYLAELQDRN EKLFFGLLME NVEELMPIVY TPTVGLACQK FGLIYRRPRG LFITINDRGH
ILDVLKNWPE ESVRCVCVTD GQRILGLGDL GAQGMGIPVG KLALYTALAG IPPYQCLPVL
LDVGTNNENL LEDPLYVGLR HKRVTGVDYD EFVDEFMEAV VRRYGQNTLI QFEDFASPNA
FKFLNKYRNQ YCTFNDDIQG TASVVLAGVQ AAQRVTGKTL PQNKFVFFGA GAAALGIASL
IAQAMVMEGL SLQQARDQIW MMDIDGLVTK DRDPKSLLGG LGHFAKDKPP LRTLIDVVNE
VKPQVLIGAS TAAGTFTPEV LNSMAKTNER PIIFALSNPT SKAECTAEQA FIHTQGRCLF
SSGSPFPPVE YEGKIYKTGQ GNNAYIFPGV ALGILATGMY HIKEEVFLIA AKAVAETLTP
AELESGTLYP PLKQIQNVSM HIAVKLCEYA YEKGLASVYP EPQDKMAWVK TKIFSYKYEP
SLPDTYQWPE ADTVKPKREI KPVTVHGVVT
//
