MAO12_PHOPR
ID MAO12_PHOPR Reviewed; 558 AA.
AC Q6LHK5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=NAD-dependent malic enzyme 2 {ECO:0000255|HAMAP-Rule:MF_01619};
DE Short=NAD-ME 2 {ECO:0000255|HAMAP-Rule:MF_01619};
DE EC=1.1.1.38 {ECO:0000255|HAMAP-Rule:MF_01619};
GN Name=maeA2 {ECO:0000255|HAMAP-Rule:MF_01619}; OrderedLocusNames=PBPRB1354;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378679; CAG23225.1; -; Genomic_DNA.
DR RefSeq; WP_011221405.1; NC_006371.1.
DR AlphaFoldDB; Q6LHK5; -.
DR SMR; Q6LHK5; -.
DR STRING; 298386.PBPRB1354; -.
DR PRIDE; Q6LHK5; -.
DR EnsemblBacteria; CAG23225; CAG23225; PBPRB1354.
DR KEGG; ppr:PBPRB1354; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_011405_5_2_6; -.
DR OMA; ADHKVYF; -.
DR OrthoDB; 654531at2; -.
DR Proteomes; UP000000593; Chromosome 2.
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; Reference proteome.
FT CHAIN 1..558
FT /note="NAD-dependent malic enzyme 2"
FT /id="PRO_0000160222"
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 411
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 558 AA; 61562 MW; 19D7E3B15F06EC81 CRC64;
MYENNKTLYL PYAGPTLLEN ALLNKGSAFS PEERQNFSLM GLLPAAIESI TEQEERAYSQ
YQTFNDDMDK HIYLRNIQDT NETLYYRLID NHIEEMMPII YTPTVGAACE QFSNIYRRGR
GLFLGYPDKG NIVDILNNAA RQDVKIIVIT DGERILGLGD QGIGGMGIPI GKLALYTACG
GINPANTLPI VLDVGTNNTQ LLSDPMYMGW RHPRITGQEY DDFVEEFIQA VKSRWPNALI
QFEDFAQKNA MPLLNRYKDK VCCFNDDIQG TAAVTVGSLL AACKAAGSEL SEQRITFVGA
GSAGCGIAEA IVAQMIAEGL SDSAARARIF MVDRWGLLTD NMQNLLDFQQ KLAQKSATVS
QWNETGNISL LDVVSNGKPT VLIGVPGLFS QEVIMEMHAH CKRPIVLPLS NPTSRVEATP
SDIIRWTEGD ALIATGSPFD PVIFNEKTYP IAQCNNSYIF PGIGLGVLAS GATRVTDEML
MESSRVLAEC SPLAQNGNGA LLPPLKDIHQ VSHCIALAVA KKAVEQNKAP QRTEKQLLEK
IESYFWKPEY LKYKRTAL
