ID A0A1S1NWW9_9GAMM Unreviewed; 426 AA.
AC A0A1S1NWW9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:OHV10503.1};
GN ORFNames=BH688_08795 {ECO:0000313|EMBL:OHV10503.1}, FY550_12875
GN {ECO:0000313|EMBL:QEL11941.1};
OS Kushneria phosphatilytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Kushneria.
OX NCBI_TaxID=657387 {ECO:0000313|EMBL:OHV10503.1, ECO:0000313|Proteomes:UP000179907};
RN [1] {ECO:0000313|EMBL:OHV10503.1, ECO:0000313|Proteomes:UP000179907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCWA18 {ECO:0000313|EMBL:OHV10503.1,
RC ECO:0000313|Proteomes:UP000179907};
RA Wang C., Qu L.;
RT "The draft genome suquence of Kushneria sp. YCWA18.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QEL11941.1, ECO:0000313|Proteomes:UP000322553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCWA18 {ECO:0000313|EMBL:QEL11941.1,
RC ECO:0000313|Proteomes:UP000322553};
RA Du G.-X., Qu L.-Y.;
RT "Complete genome sequence of Kushneria sp. YCWA18, a halophilic phosphate-
RT solubilizing bacterium isolated from Daqiao saltern in China.";
RL Submitted (AUG-2019) 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; MKZT01000012; OHV10503.1; -; Genomic_DNA.
DR EMBL; CP043420; QEL11941.1; -; Genomic_DNA.
DR RefSeq; WP_070978510.1; NZ_MKZT01000012.1.
DR AlphaFoldDB; A0A1S1NWW9; -.
DR STRING; 657387.BH688_08795; -.
DR KEGG; kuy:FY550_12875; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000179907; Unassembled WGS sequence.
DR Proteomes; UP000322553; Chromosome.
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:UP000179907}.
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 426 AA; 45789 MW; 807F9D89A4833B1E CRC64;
MSDSRRQEAL DYHARPIPGK LSVELTKPTH SQKHLALAYS PGVAEPVREI ARDPENAYRY
TGKGNLVAVI SNGSAILGLG NLGALASKPV MEGKGVLFKR FAGINAVDIE VDVAEPQAFI
DTVTHIADSW GGINLEDIKA PECFEIENAL KQRCSIPVFH DDQHGTAIVT AAGLLNALEI
AGKSLESAHI VCLGAGSAAI ACMKLLIEMG ARNEQIDMLD SKGVIHSGRS DLNPYKAQFA
TETEHRTLDD AIEGADVFIG LSGPNLLSTE QLKRMGANPI VFACSNPDPE IHPDEAHAAR
DDVIMATGRS DYPNQVNNVL GFPFIFRGAL DVRASDITEA MKIAAVHALR NIAREPVTRE
VLEAYELDSL EFGRGYIIPT PVDSRLLGRV SSAVAQAAID SNVATRGYPE HYPLQGVDDI
YGGTNH
//
