ID A0A0F6AH15_9GAMM Unreviewed; 564 AA.
AC A0A0F6AH15;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=NAD-dependent malic enzyme {ECO:0000256|HAMAP-Rule:MF_01619};
DE Short=NAD-ME {ECO:0000256|HAMAP-Rule:MF_01619};
DE EC=1.1.1.38 {ECO:0000256|HAMAP-Rule:MF_01619};
GN Name=maeA {ECO:0000256|HAMAP-Rule:MF_01619};
GN ORFNames=N479_07770 {ECO:0000313|EMBL:KKE84684.1};
OS Pseudoalteromonas luteoviolacea S4054.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1129367 {ECO:0000313|EMBL:KKE84684.1, ECO:0000313|Proteomes:UP000033434};
RN [1] {ECO:0000313|EMBL:KKE84684.1, ECO:0000313|Proteomes:UP000033434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4054 {ECO:0000313|EMBL:KKE84684.1,
RC ECO:0000313|Proteomes:UP000033434};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_01619};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01619,
CC ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01619,
CC ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|HAMAP-Rule:MF_01619, ECO:0000256|PIRSR:PIRSR000106-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01619}.
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|HAMAP-Rule:MF_01619,
CC ECO:0000256|RuleBase:RU003427}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKE84684.1}.
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DR EMBL; AUXW01000113; KKE84684.1; -; Genomic_DNA.
DR RefSeq; WP_046355076.1; NZ_AUXW01000113.1.
DR AlphaFoldDB; A0A0F6AH15; -.
DR PATRIC; fig|1129367.4.peg.1297; -.
DR Proteomes; UP000033434; Unassembled WGS sequence.
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 GO; GO:0008152; P: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 HAMAP; MF_01619; NAD_malic_enz; 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 InterPro; IPR023667; NAD_malic_enz_proteobac.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF32; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01619};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01619};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01619}.
FT DOMAIN 80..260
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 270..530
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 103
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 245
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 246
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619"
FT BINDING 269
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 417
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT SITE 269
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619"
SQ SEQUENCE 564 AA; 62916 MW; AFABCAC316AA2EDB CRC64;
MTKQTDPNYL YIPYSGPTLL ETPLLNKGSA FSQRERENFN LAGLVPPRYE TIEEQVERCY
QQFSSFKDNL NKHIYLRAIQ DNNETLYYRL VRDHLEEMMP IIYTPTVGDA CEKFSDIYRS
SRGLFISYED RHNIDDILRN ATKGKVKVIV VTDGERILGL GDQGIGGMGI PIGKLALYTV
CGGISPAYTL PVMLDVGTNN EKLLNDPMYM GARHKRINQE EYDEFLDLFI KAVKRRWPNV
LLQFEDFAQP NAMPLLKRYR DEICCFNDDI QGTASVTVGS LLAACRVKGA KLSEQKVVFV
GAGSAGCGIA EQIIAQMVSE GVSDEQARSQ VFMVDRFGLL TEGMEGLRDF QAALVQTSTN
LENWNYSGEY ASLLDVMHCA QPDILIGVSG QPGLFTEQVI KAMHSGCDQP IIFPLSNPSR
QVEAHPKDVI EWTLGQAIVA TGSPFEPVEF GGETYVIPQC NNSYIFPGIG LGALAAKASR
ITESMLMVAS ETLAESSPWA NTGKGSLLPS LVEIEQLSKR IAFAVAKKAM EEGVCLDMPD
ERIWATIEQN YWMPEYRNYK RCSI
//
