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Database: UniProt
Entry: A0A0C5WQF5_9GAMM
LinkDB: A0A0C5WQF5_9GAMM
Original site: A0A0C5WQF5_9GAMM 
ID   A0A0C5WQF5_9GAMM        Unreviewed;       416 AA.
AC   A0A0C5WQF5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Putative malate oxidoreductase {ECO:0000313|EMBL:AJR07254.1};
GN   ORFNames=H744_2c0518 {ECO:0000313|EMBL:AJR07254.1};
OS   Photobacterium gaetbulicola Gung47.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR07254.1, ECO:0000313|Proteomes:UP000032303};
RN   [1] {ECO:0000313|EMBL:AJR07254.1, ECO:0000313|Proteomes:UP000032303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gung47 {ECO:0000313|EMBL:AJR07254.1,
RC   ECO:0000313|Proteomes:UP000032303};
RA   Kim Y.-O.;
RT   "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT   gaetbulicola Gung47.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP005974; AJR07254.1; -; Genomic_DNA.
DR   RefSeq; WP_039469059.1; NZ_CP005974.1.
DR   AlphaFoldDB; A0A0C5WQF5; -.
DR   STRING; 658445.H744_2c0518; -.
DR   KEGG; pgb:H744_2c0518; -.
DR   PATRIC; fig|658445.3.peg.2423; -.
DR   HOGENOM; CLU_034446_2_1_6; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000032303; Chromosome 2.
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:UP000032303}.
FT   DOMAIN          18..151
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          163..399
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        39
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        94
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         136
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         137
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         162
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   416 AA;  44969 MW;  DD6FF43FC58F2914 CRC64;
     MSEDFRQQAL HYHAYPVPGK IAVELTKPAN TVEDLALAYS PGVAEPVREI AQNAENVYKY
     TGKGNMVAVI TNGTAILGLG NLGPLASKPV MEGKALLFKR FAGLDSIDIE VKHRTIDEFV
     DTVANIADTF GGINLEDIKA PDCFEIEKRL IERCHVPVFH DDQHGTAIVT AAGMLNALEL
     QGKKISEAVI VCLGAGAAAV ACMELLIKCG AQREKIYMLD RKGVIHTRRD DINEYKQLFA
     NNTDKRTLED VIEGADIFVG VSGPDLLAPE ALKLMADKPV VFACSNPDPE IKPELAHAVR
     DDLIMGTGRS DYPNQVNNVI CFPFIFRGAL DVRASEINDE MKLAAVDAIR ALAKEPVPAE
     VIAAAGADKL EFGPDYIIPK PMDPRLLPRV AKAVAQAAVE SGVAQIDMPA GYMEAK
//
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