ID   A0A252B9I0_9PROT        Unreviewed;       542 AA.
AC   A0A252B9I0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:OUJ00870.1};
GN   ORFNames=HK20_05535 {ECO:0000313|EMBL:OUJ00870.1};
OS   Acetobacter sp. DsW_54.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=1670660 {ECO:0000313|EMBL:OUJ00870.1, ECO:0000313|Proteomes:UP000194822};
RN   [1] {ECO:0000313|EMBL:OUJ00870.1, ECO:0000313|Proteomes:UP000194822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DsW_54 {ECO:0000313|EMBL:OUJ00870.1};
RA   Ju J., Zhang J.;
RL   Submitted (JUN-2014) 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, ECO:0000256|RuleBase:RU003427}.
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:OUJ00870.1}.
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DR   EMBL; JOPD01000001; OUJ00870.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A252B9I0; -.
DR   Proteomes; UP000194822; 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   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   CDD; cd05312; NAD_bind_1_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; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR   PANTHER; PTHR23406:SF90; MALIC ENZYME-RELATED; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 1.
DR   PRINTS; PR00072; MALOXRDTASE.
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   ECO:0000256|RuleBase:RU003427};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194822}.
FT   DOMAIN          73..253
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          263..514
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        96
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         238
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         239
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         262
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         445
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   542 AA;  59927 MW;  B445AAFC4B05C042 CRC64;
     MPSALTLRGT ALLNNALLNK GTAFTEAERR EYGLEGLLPT QVETLDRQVE RIHRHLEAKP
     SNLERYIYLS GLRDQNQTLF YRVLMSNPAQ FVPIVYAPTL AAVCQQFSHI YRRPRGMYIS
     LDMRGRIRDV LRNWPTDNVR FLCVTTGGRI LGLGDIGVNG MGIPIGKLDL YTACGAVPPE
     VLLPVQLDIG TTNSALRADP LYLGLRREPP PLEELDGFVE EFVSAVKEVF PNCCLHFEDW
     KGTDALHYLD KYRNTALCYN DDIQGTAAVT LAGLITALKI KNETLAQQRF LFLGAGSSGL
     GTADMLISAL KQEGISEQEA IERITLMDVN GLLETSRTDL SPQQKRYAKA MPPSRDLLAT
     IKAIKPTVLI GVSTSGGAFT QEVVETMSAL NERPIIFPLS LPQKNAECTA EQAYEWSQGQ
     ALFAAGLQFP EVEMNGRTFY PGQANNFYIF PALGLAVYAT CPKHITDDMV IETARALADQ
     VDPASRERGR LFPPQSDILE VSVTSAARIA EFIFDQGAAT VERPKDIRAW IESLTYSPRY
     AG
//