ID A0A208Y9U9_9BURK Unreviewed; 426 AA.
AC A0A208Y9U9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Malate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CDO44_01480 {ECO:0000313|EMBL:OVZ64903.1};
OS Pigmentiphaga sp. NML080357.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pigmentiphaga.
OX NCBI_TaxID=2008675 {ECO:0000313|EMBL:OVZ64903.1, ECO:0000313|Proteomes:UP000196551};
RN [1] {ECO:0000313|EMBL:OVZ64903.1, ECO:0000313|Proteomes:UP000196551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML080357 {ECO:0000313|EMBL:OVZ64903.1,
RC ECO:0000313|Proteomes:UP000196551};
RA Bernier A.-M., Bernard K.;
RT "Pigmentiphaga species Genome sequencing and assembly.";
RL Submitted (MAY-2017) 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 -!- 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:OVZ64903.1}.
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DR EMBL; NINW01000003; OVZ64903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A208Y9U9; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000196551; 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; 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; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 18..151
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 163..400
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 287
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 426 AA; 45660 MW; 189A7F19E8801910 CRC64;
MDSSLTDKAL AYHQFPVPGK IAVVPTKPLD NQQDLSLAYS PGVAAACEAI ANEQQATRYY
TSRSNLVAVI SNGTAVLGLG NIGPYAAKPV MEGKACLFQK FAGINVFDIE LAETDPDKLV
DAIAMMEPTF GGINLEDIKA PECFYIERKL TERMSIPVFH DDQHGTAIVA SAGIVNGLKL
AEKSLDRVKL VCSGAGAAAI ACLDLLVRQG LKKENILLVD SKGVVYEGRD ASMEFNKSRY
ATTSTARTLA DAVKDADIFL GCSAAGLLTP DMVATMALRP LILALANPEP EIRPELAREV
RSDCLIATGR SDYPNQVNNV LCFPFLFRGA LDVDAMRITD EMKLACVNAI ANLAQQPIPP
EVAKAYPNRK LEFGPDYFIP TPFDPRLISE VAAAVALAAM DSGVARSPIA DIDAYRESLA
SSSSNR
//
