ID U5L5A7_9BACI Unreviewed; 564 AA.
AC U5L5A7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:AGX02944.1};
DE EC=1.1.1.38 {ECO:0000313|EMBL:AGX02944.1};
GN ORFNames=N288_04940 {ECO:0000313|EMBL:AGX02944.1};
OS Bacillus infantis NRRL B-14911.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1367477 {ECO:0000313|EMBL:AGX02944.1, ECO:0000313|Proteomes:UP000017805};
RN [1] {ECO:0000313|EMBL:AGX02944.1, ECO:0000313|Proteomes:UP000017805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-14911 {ECO:0000313|EMBL:AGX02944.1,
RC ECO:0000313|Proteomes:UP000017805};
RA Massilamany C., Smith T.P.L., Loy J.D., Barletta R., Reddy J.;
RT "Complete genome sequence of Bacillus infantis NRRL B-14911 that has
RT potential to induce cardiac disease by antigenic mimicry.";
RL Submitted (JUL-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, ECO:0000256|RuleBase:RU003427}.
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DR EMBL; CP006643; AGX02944.1; -; Genomic_DNA.
DR RefSeq; WP_009791885.1; NC_022524.1.
DR AlphaFoldDB; U5L5A7; -.
DR STRING; 1367477.N288_04940; -.
DR GeneID; 85551001; -.
DR KEGG; bif:N288_04940; -.
DR PATRIC; fig|1367477.3.peg.920; -.
DR HOGENOM; CLU_011405_5_2_9; -.
DR OrthoDB; 3314528at2; -.
DR Proteomes; UP000017805; 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; 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; 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; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF32; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 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 Oxidoreductase {ECO:0000313|EMBL:AGX02944.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017805}.
FT DOMAIN 81..263
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 273..533
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 104
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 248
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 249
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 272
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 421
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 465
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 564 AA; 62087 MW; 5049B37D65C4BE45 CRC64;
MTASDGAKNV IYTDLRGKEL LSNPYLNKGV AFTKEERDDL GLQGLLPTQV LTLDEQATRA
YEQFSRRTNN MFKNGVLYDL YNRNVVLFYR LLRDHLNEML PIIYTPTVGE AIQRYSHEYH
RPGGLYLTIE DPEEMDKAFE NLNKPHEGID LIVVTDSESI LGIGDQGVGG INIAIGKLAV
YTAAAGIDPS RVLPVVLDVG TNNEDLINDP LYIGNKFPRV RGERYEQFVD QFVVTARKFF
PNVLLHWEDL GNVNARNIME KYGNEILTFN DDIQGTGAVT LAAVMSALKV TGGSLKDQRI
LVFGPGAAGI GNADQMAETM ILEGLDREEA YDRFWAFDYR GLLTEETPDV LKFQKPYVRS
AEEVKDWERD GADTIPLLEV VKRVKPTILI GTSGQAGAFT EEIVREMAKH VERPIIMPMS
NPTLLAEAVP EDLFNWTDGK ALIATGSPFA NVEYNGISHE IGQSNNAFVF PGLGLGAIVA
KAEIISKGMF AAAANAVAEK SDSSTPGASL LPAITKLADV SRHVAIEVAK AAVQEGIAKA
EIDDIEQAVD DAMWKPEYKQ IKSK
//
