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Database: UniProt
Entry: A0A2N0WQS0_9GAMM
LinkDB: A0A2N0WQS0_9GAMM
Original site: A0A2N0WQS0_9GAMM 
ID   A0A2N0WQS0_9GAMM        Unreviewed;       414 AA.
AC   A0A2N0WQS0;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:PKF56782.1};
GN   ORFNames=CW748_08575 {ECO:0000313|EMBL:PKF56782.1};
OS   Alteromonadales bacterium alter-6D02.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales.
OX   NCBI_TaxID=2058087 {ECO:0000313|EMBL:PKF56782.1, ECO:0000313|Proteomes:UP000233605};
RN   [1] {ECO:0000313|EMBL:PKF56782.1, ECO:0000313|Proteomes:UP000233605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=alter-6D02 {ECO:0000313|Proteomes:UP000233605};
RX   PubMed=27311813; DOI=.1038/ncomms11965;
RA   Datta M.S., Sliwerska E., Gore J., Polz M.F., Cordero O.X.;
RT   "Microbial interactions lead to rapid micro-scale successions on model
RT   marine particles.";
RL   Nat. Commun. 7:11965-11965(2016).
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785}.
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:PKF56782.1}.
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DR   EMBL; PIZK01000013; PKF56782.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N0WQS0; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000233605; Unassembled WGS sequence.
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; cd05311; NAD_bind_2_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; 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; IPR045213; Malic_NAD-bd_bact_type.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43237; NADP-DEPENDENT MALIC ENZYME; 1.
DR   PANTHER; PTHR43237:SF4; NADP-DEPENDENT MALIC ENZYME; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 1.
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,
KW   ECO:0000256|PIRSR:PIRSR000106-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233605}.
FT   DOMAIN          17..150
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          162..398
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        38
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        93
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         135
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         136
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         161
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   414 AA;  44923 MW;  784EF65662D79865 CRC64;
     MTDFRQQALD YHAQPTPGKI SVELSTPAET AQDLALAYSP GVAEPVREIA QDPENAYKYT
     AKGNLVAVIT NGTAILGLGN LGPLASKPVM EGKALLFKRF ANIDSIDIEV KHRTVDEFVD
     TVANIADTFG GINLEDIKAP ECFMIEKALK ERCSIPVFHD DQHGTAIVTA AGMINALDIQ
     GKKIEESVIV CMGAGAAAVS CMELLISCGA MREKIYMLDR KGVIHASRDD LNEYKRRFAN
     NTDMRTLEEV INGADIFVGV SGPDVITADH VKLMAPNPVI FACSNPDPEI KPELAHEARS
     DLIMATGRSD YPNQVNNVLC FPFIFRGALD VRASTINEEM KVAAVHAIRQ IAKEPVSKEV
     LKASGHKELS FGKEYIIPKP MDPRLLTRVS RAVAQAAIDS GVAGIEMPEG YMAE
//
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