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Database: UniProt
Entry: A0A075JMX1_9BACI
LinkDB: A0A075JMX1_9BACI
Original site: A0A075JMX1_9BACI 
ID   A0A075JMX1_9BACI        Unreviewed;       411 AA.
AC   A0A075JMX1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=NAD-dependent malic enzyme 4 {ECO:0000313|EMBL:AIF43219.1};
GN   ORFNames=X953_08685 {ECO:0000313|EMBL:AIF43219.1};
OS   Virgibacillus sp. SK37.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=403957 {ECO:0000313|EMBL:AIF43219.1, ECO:0000313|Proteomes:UP000027985};
RN   [1] {ECO:0000313|EMBL:AIF43219.1, ECO:0000313|Proteomes:UP000027985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK37 {ECO:0000313|EMBL:AIF43219.1,
RC   ECO:0000313|Proteomes:UP000027985};
RA   Phrommao E., Yongsawatdigul J., Rodtong S., Steele J.L.;
RT   "Complete genome sequence of Virgibacillus sp. SK37, a moderately
RT   halophilic bacterium isolated from Thai fish sauce fermentation.";
RL   Submitted (FEB-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, ECO:0000256|RuleBase:RU003427}.
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DR   EMBL; CP007161; AIF43219.1; -; Genomic_DNA.
DR   RefSeq; WP_040955128.1; NZ_CP007161.1.
DR   AlphaFoldDB; A0A075JMX1; -.
DR   STRING; 403957.X953_08685; -.
DR   KEGG; vir:X953_08685; -.
DR   HOGENOM; CLU_034446_2_1_9; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000027985; Chromosome.
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   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.
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:UP000027985}.
FT   DOMAIN          16..149
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          161..385
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        37
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        92
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         134
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         135
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         160
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         317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   411 AA;  44224 MW;  A687ECF57A0EA5BB CRC64;
     MASLRDEALH IHKVNKGKLT TNSKIPVRNA KDLSLAYSPG VAEPCKEIYE RKETVYDYTM
     KGNMVAVVSD GSAVLGLGNI GPEAALPVME GKSVLFKSFA GVDSFPICLN THDIEEIVQT
     VKLMEPTFGG VNLEDIAAPN CFVIEERLKK ETNIPIFHDD QHGTAIVTVA GLINALKLVG
     KSFSDIKVVA NGAGAAGIAI IKLLYSFGVR EMIMCDSKGA IFEDRPYGMN EVKENVAKFT
     NLAKKEGSLE EMLEDADVFI GVSVGGALTP EMVKKMNEDA IIFAMANPDP EIMPENAKEA
     GARVIGTGRS DFPNQVNNVL AFPGIFRGAL DVRATRINEK MKIAAAEAIA SLIGDGELNE
     DYVIPAPFDA RVAPIVAKSV AQAAMESGVA RIDVDPEEIA EKTRRLTQID Q
//
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