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MAO1_VIBVU
ID   MAO1_VIBVU              Reviewed;         562 AA.
AC   Q8D911;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=NAD-dependent malic enzyme {ECO:0000255|HAMAP-Rule:MF_01619};
DE            Short=NAD-ME {ECO:0000255|HAMAP-Rule:MF_01619};
DE            EC=1.1.1.38 {ECO:0000255|HAMAP-Rule:MF_01619};
GN   Name=maeA {ECO:0000255|HAMAP-Rule:MF_01619}; OrderedLocusNames=VV1_2801;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = CO2 + NADH + pyruvate;
CC         Xref=Rhea:RHEA:12653, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.38;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01619};
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=1.1.1.38; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01619};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01619};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01619};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000255|HAMAP-Rule:MF_01619};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01619}.
CC   -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000255|HAMAP-
CC       Rule:MF_01619}.
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DR   EMBL; AE016795; AAO11140.1; -; Genomic_DNA.
DR   RefSeq; WP_011080634.1; NC_004459.3.
DR   AlphaFoldDB; Q8D911; -.
DR   SMR; Q8D911; -.
DR   EnsemblBacteria; AAO11140; AAO11140; VV1_2801.
DR   KEGG; vvu:VV1_2801; -.
DR   PATRIC; fig|196600.6.peg.1449; -.
DR   HOGENOM; CLU_011405_5_2_6; -.
DR   OMA; QMWDPVY; -.
DR   Proteomes; UP000002275; Chromosome 1.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-UniRule.
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-UniRule.
DR   Gene3D; 3.40.50.10380; -; 1.
DR   HAMAP; MF_01619; NAD_malic_enz; 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   InterPro; IPR023667; NAD_malic_enz_proteobac.
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   3: Inferred from homology;
KW   Metal-binding; NAD; Oxidoreductase.
FT   CHAIN           1..562
FT                   /note="NAD-dependent malic enzyme"
FT                   /id="PRO_0000160237"
FT   ACT_SITE        101
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         154
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         243
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         244
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         267
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         267
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         415
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   SITE            267
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
SQ   SEQUENCE   562 AA;  62088 MW;  F05F1BC579ABBAB1 CRC64;
     MNNDKRPLYI PFAGPALLST PLLNKGSAFS AEERISFNLE GLLPETTETI QEQVERAYMQ
     YKAFESDMDK HIYLRNIQDT NETLFYRLVQ NHITEMMPII YTPTVGAACE NFSNIYRRGR
     GLFVSYANRD RIDDILNNAS NHNVKVIVVT DGERILGLGD QGIGGMGIPI GKLSLYTACG
     GISPAYTLPI VLDVGTNNPQ RLADPMYMGW RHPRITGADY DAFVEEFIQA VQRRWPDALI
     QFEDFAQKNA MPLLERYKNR ICCFNDDIQG TAAVTVGSLM AACQAAGSKL SEQRITFLGA
     GSAGCGIAEA IIAQMVSEGI SDKKARSQVF MVDRWGLLQE GMPNLLDFQQ RLVQKHSVTA
     KWETEANGFS LLDVVKNAKP TVLIGVSGAP GLFTQEVIQE MHKHCPRPIV FPLSNPTSRV
     EAVPADIIRW TNGDALVATG SPFDPVIHEG KTYPIVQCNN SYIFPGIGLG VLAVNAKRVT
     DEMLMESSRA LATCSPLAIN GKGALLPPLE EIHTVSKRIA YAVAKKAIEQ GVALEIADDA
     LQVAIEQHFW QPVYRRYKRT AF
 
 
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