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Database: UniProt
Entry: A0A0B0IIJ3_9BACI
LinkDB: A0A0B0IIJ3_9BACI
Original site: A0A0B0IIJ3_9BACI 
ID   A0A0B0IIJ3_9BACI        Unreviewed;       396 AA.
AC   A0A0B0IIJ3;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KHF39496.1};
GN   ORFNames=LQ50_14640 {ECO:0000313|EMBL:KHF39496.1};
OS   Halalkalibacter okhensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX   NCBI_TaxID=333138 {ECO:0000313|EMBL:KHF39496.1, ECO:0000313|Proteomes:UP000030832};
RN   [1] {ECO:0000313|EMBL:KHF39496.1, ECO:0000313|Proteomes:UP000030832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kh10-101T {ECO:0000313|Proteomes:UP000030832};
RA   Prakash J.S.;
RT   "Genome sequencing and annotation of Bacillus Okhensis strain Kh10-101T.";
RL   Submitted (SEP-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   -!- 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}.
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:KHF39496.1}.
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DR   EMBL; JRJU01000018; KHF39496.1; -; Genomic_DNA.
DR   RefSeq; WP_034630333.1; NZ_JRJU01000018.1.
DR   AlphaFoldDB; A0A0B0IIJ3; -.
DR   STRING; 333138.LQ50_14640; -.
DR   eggNOG; COG0281; Bacteria.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000030832; Unassembled WGS sequence.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
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   Reference proteome {ECO:0000313|Proteomes:UP000030832}.
FT   DOMAIN          18..151
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          163..386
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         288
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   396 AA;  42246 MW;  98851E97DB29F9A8 CRC64;
     MKHKNLKEQA IQLHRQHAGK IEVVSKVEIN SEAELSLVYT PGVGDVCKEI EKNPHEINHL
     TSRGNMVAVV TDGTAVLGLG DIGPGAAMPV MEGKCMLFKN FANIDAFPIC LDTKNVDEIV
     ATVKALQPTF AGINLEDISA PRCFEIEDRL KKDLDIPVFH DDQHGTAIVV LAGLINGLKV
     VGKQMKAVKI VINGAGAAGI SIAKLLLHAG FTNITLVSLE GVVNQSEGWL NSSQLQIAKV
     TNRENVRGTL KDAILHADVF IGVSGPAALK AEYVKSMAKD PIVFAMANPI PEIYPEEALA
     AGAKVVGTGR SDYPNQINNL LAFPGIFRGA IDSQASDITT DMKIAAAFAI ANVIPEKELS
     PEYVIPNALN KEVPKVVAEA VAKSALEKDR VTIKSS
//
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