ID W0E7S9_MARPU Unreviewed; 424 AA.
AC W0E7S9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:AHF05121.1};
GN ORFNames=MARPU_15680 {ECO:0000313|EMBL:AHF05121.1};
OS Marichromatium purpuratum 984.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Marichromatium.
OX NCBI_TaxID=765910 {ECO:0000313|EMBL:AHF05121.1, ECO:0000313|Proteomes:UP000005275};
RN [1] {ECO:0000313|EMBL:AHF05121.1, ECO:0000313|Proteomes:UP000005275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=984 {ECO:0000313|EMBL:AHF05121.1,
RC ECO:0000313|Proteomes:UP000005275};
RG DOE Joint Genome Institute;
RA Bryant D.A., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-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; CP007031; AHF05121.1; -; Genomic_DNA.
DR RefSeq; WP_005222922.1; NZ_CP007031.1.
DR AlphaFoldDB; W0E7S9; -.
DR STRING; 765910.MARPU_15680; -.
DR KEGG; mpur:MARPU_15680; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_034446_2_1_6; -.
DR Proteomes; UP000005275; 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; 2.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 2.
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:UP000005275}.
FT DOMAIN 27..160
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 172..409
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 48
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 145
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 146
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 171
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 424 AA; 45625 MW; 59F21427F6E8A76C CRC64;
MTDPESFAHH DADLNKQALA YHAEPRPGKI GIEVTKSAST QHELSLAYTP GVAEPVRHIH
DDPENAYRYT NKGNLVAVIT DGSAVLGLGK VGAQASKPVM EGKSVLFKRF ADIDCFDIEV
EARHPQAFIE TVVRIAPTFG GINLEDIAAP HCFEIEQALI EQLDIPVFHD DQHGTAIIIA
AGLLNALELQ GKSLAEARIV VLGAGAAGIA AIRLLLALGA HRDNIFAIDR QGVIHVGRQD
LNPYKFGIAA DTERRTLADA MDGADAFIGV SGPDLVTADM LASMAPRPVV FALSNPVPEV
RPALAREVRD DLIMATGRSD YPNQINNVLG FPFIFRGALD VRASRINENM QIAAVEALRA
ITREPVPAEV LAAYEGLESL EFGPDYIIPK PFDPRLRERV SAAVARAAIE SGVARAPYPA
HYPG
//
