MAOX_COLLI
ID MAOX_COLLI Reviewed; 557 AA.
AC P40927;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=NADP-dependent malic enzyme;
DE Short=NADP-ME;
DE EC=1.1.1.40;
GN Name=ME1;
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8161199; DOI=10.1006/abbi.1994.1152;
RA Chou W.-Y., Huang S.-M., Liu Y.H., Chang G.-G.;
RT "Cloning and expression of pigeon liver cytosolic NADP(+)-dependent malic
RT enzyme cDNA and some of its abortive mutants.";
RL Arch. Biochem. Biophys. 310:158-166(1994).
RN [2]
RP PROTEIN SEQUENCE OF 259-283.
RX PubMed=8011656; DOI=10.1021/bi00191a021;
RA Wei C.H., Chou W.-Y., Huang S.-M., Lin C.C., Chang G.-G.;
RT "Affinity cleavage at the putative metal-binding site of pigeon liver malic
RT enzyme by the Fe(2+)-ascorbate system.";
RL Biochemistry 33:7931-7936(1994).
RN [3]
RP MUTAGENESIS OF LYS-162 AND LYS-340.
RX PubMed=10772909; DOI=10.1006/bbrc.2000.2502;
RA Kuo C.C., Tsai L.C., Chin T.Y., Chang G.G., Chou W.Y.;
RT "Lysine residues 162 and 340 are involved in the catalysis and coenzyme
RT binding of NADP(+)-dependent malic enzyme from pigeon.";
RL Biochem. Biophys. Res. Commun. 270:821-825(2000).
RN [4]
RP MUTAGENESIS OF ASP-141; ASP-194 AND ASP-464.
RX PubMed=10716176; DOI=10.1110/ps.9.2.242;
RA Chou W.Y., Chang H.P., Huang C.H., Kuo C.C., Tong L., Chang G.G.;
RT "Characterization of the functional role of Asp141, Asp194, and Asp464
RT residues in the Mn2+-L-malate binding of pigeon liver malic enzyme.";
RL Protein Sci. 9:242-251(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-556 IN COMPLEX WITH NADP;
RP MANGANESE AND SUBSTRATE ANALOG, AND SUBUNIT.
RX PubMed=11790843; DOI=10.1110/ps.38002;
RA Yang Z., Zhang H., Huang H.-C., Kuo C.-C., Tsai L.-C., Yuan H.S.,
RA Chou W.-Y., Chang G.-G., Tong L.;
RT "Structural studies of the pigeon cytosolic NADP(+)-dependent malic
RT enzyme.";
RL Protein Sci. 11:332-341(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NADP(+) = CO2 + NADPH + pyruvate;
CC Xref=Rhea:RHEA:18253, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.40;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:16526; EC=1.1.1.40;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Divalent metal cations. Prefers magnesium or manganese.;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11790843}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR EMBL; L09233; AAA49450.1; -; mRNA.
DR PIR; S43231; S43231.
DR RefSeq; NP_001269745.1; NM_001282816.1.
DR PDB; 1GQ2; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=2-556.
DR PDBsum; 1GQ2; -.
DR AlphaFoldDB; P40927; -.
DR SMR; P40927; -.
DR STRING; 8932.XP_005506781.1; -.
DR GeneID; 102096434; -.
DR KEGG; clv:102096434; -.
DR CTD; 4199; -.
DR eggNOG; KOG1257; Eukaryota.
DR OrthoDB; 435571at2759; -.
DR SABIO-RK; P40927; -.
DR EvolutionaryTrace; P40927; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.10380; -; 1.
DR InterPro; IPR046346; Aminiacid_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 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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Manganese;
KW Metal-binding; NADP; Oxidoreductase.
FT CHAIN 1..557
FT /note="NADP-dependent malic enzyme"
FT /id="PRO_0000160198"
FT ACT_SITE 91
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:11790843"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:11790843"
FT BINDING 144
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11790843"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11790843"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11790843"
FT BINDING 234
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:11790843"
FT BINDING 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:11790843"
FT BINDING 238
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11790843"
FT BINDING 258
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:11790843"
FT BINDING 291..294
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11790843"
FT BINDING 325
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11790843"
FT BINDING 397
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11790843"
FT BINDING 443
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11790843"
FT BINDING 443
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11790843"
FT SITE 258
FT /note="Important for activity"
FT SITE 340
FT /note="Confers specificity for NADP"
FT MUTAGEN 141
FT /note="D->N: Increases Km for manganese 14-fold. Increases
FT Km for malate 5-fold."
FT /evidence="ECO:0000269|PubMed:10716176"
FT MUTAGEN 162
FT /note="K->A: Decreases kcat 235-fold. no effect on Km for
FT NADP."
FT /evidence="ECO:0000269|PubMed:10772909"
FT MUTAGEN 194
FT /note="D->N: No effect on Km for manganese. Increases Km
FT for malate 8-fold."
FT /evidence="ECO:0000269|PubMed:10716176"
FT MUTAGEN 340
FT /note="K->A: Increases Km for NADP 65-fold. No effect on
FT kcat."
FT /evidence="ECO:0000269|PubMed:10772909"
FT MUTAGEN 464
FT /note="D->N: No effect."
FT /evidence="ECO:0000269|PubMed:10716176"
FT CONFLICT 279
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:1GQ2"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 21..26
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1GQ2"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:1GQ2"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1GQ2"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1GQ2"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 189..193
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 208..225
FT /evidence="ECO:0007829|PDB:1GQ2"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 238..248
FT /evidence="ECO:0007829|PDB:1GQ2"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:1GQ2"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:1GQ2"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 260..277
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:1GQ2"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 293..308
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 313..317
FT /evidence="ECO:0007829|PDB:1GQ2"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 353..360
FT /evidence="ECO:0007829|PDB:1GQ2"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 377..386
FT /evidence="ECO:0007829|PDB:1GQ2"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 406..412
FT /evidence="ECO:0007829|PDB:1GQ2"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:1GQ2"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 447..457
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 464..476
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 480..484
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 495..512
FT /evidence="ECO:0007829|PDB:1GQ2"
FT HELIX 525..530
FT /evidence="ECO:0007829|PDB:1GQ2"
FT STRAND 550..553
FT /evidence="ECO:0007829|PDB:1GQ2"
SQ SEQUENCE 557 AA; 62054 MW; 7489A2E6741567C8 CRC64;
MKKGYEVLRD PHLNKGMAFT LEERQQLNIH GLLPPCFLGQ DAQVYSILKN FERLTSDLDR
YILLMSLQDR NEKLFYKVLT SDIERFMPIV YTPTVGLACQ HYGLAFRRPR GLFITIHDRG
HIATMLQSWP ESVIKAIVVT DGERILGLGD LGCYGMGIPV GKLALYTACG GVKPHQCLPV
MLDVGTDNET LLKDPLYIGL RHKRIRGQAY DDLLDEFMEA VTSRYGMNCL IQFEDFANAN
AFRLLHKYRN KYCTFNDDIQ GTASVAVAGL LAALRITKNR LSDHTVLFQG AGEAALGIAN
LIVMAMQKEG VSKEEAIKRI WMVDSKGLIV KGRASLTPEK EHFAHEHCEM KNLEDIVKDI
KPTVLIGVAA IGGAFTQQIL QDMAAFNKRP IIFALSNPTS KAECTAEQLY KYTEGRGIFA
SGSPFDPVTL PSGQTLYPGQ GNNSYVFPGV ALGVISCGLK HIGDDVFLTT AEVIAQEVSE
ENLQEGRLYP PLVTIQQVSL KIAVRIAKEA YRNNTASTYP QPEDLEAFIR SQVYSTDYNC
FVADSYTWPE EAMKVKL
