ID B2HL83_MYCMM Unreviewed; 548 AA.
AC B2HL83;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=[NAD] dependent malate oxidoreductase Mez {ECO:0000313|EMBL:ACC42059.1};
GN Name=mez {ECO:0000313|EMBL:ACC42059.1};
GN OrderedLocusNames=MMAR_3643 {ECO:0000313|EMBL:ACC42059.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC42059.1, ECO:0000313|Proteomes:UP000001190};
RN [1] {ECO:0000313|EMBL:ACC42059.1, ECO:0000313|Proteomes:UP000001190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
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}.
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DR EMBL; CP000854; ACC42059.1; -; Genomic_DNA.
DR RefSeq; WP_012395267.1; NC_010612.1.
DR AlphaFoldDB; B2HL83; -.
DR STRING; 216594.MMAR_3643; -.
DR KEGG; mmi:MMAR_3643; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_011405_5_2_11; -.
DR OrthoDB; 3314528at2; -.
DR Proteomes; UP000001190; Chromosome.
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 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: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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW ECO:0000256|RuleBase:RU003427};
KW Reference proteome {ECO:0000313|Proteomes:UP000001190}.
FT DOMAIN 73..255
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 265..522
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 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 240
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 241
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 264
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 454
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 548 AA; 59124 MW; 8CCA9BCE81F1B00F CRC64;
MSDARVPRFP DALSTPSLNR GVGFTHEQRR ALGLTGRLPA AVLTLDQQSE RVWHQLQSLA
TDLGRNLLLE QLHYRHELLY YKVLTEHLVE LMPVVYTPTV GEAIQRFSDE YRGQRGLFLS
IDEPDEIAAA FETFGLGPDD VDLIVCTDAE AILGIGDWGV GGIQIAVGKL ALYTAGGGID
PRRSLAVSLD VGTDNEQLLQ DPFYLGNRHA RRRGEEYDQF IKRYIEIAHR LFPRAMLHFE
DFGPTNARMI LRTYGADYCV FNDDVQGTGA VVVAAIDGGS HVTGVPVRDN TVIVFGAGTA
GVGVADQIRD AMVADGATVE QATSQIWAVD KQGLLFDDMA DLREFQVPYA KNRARLGVGA
SDRVGLVDAI KLAAPTVLLG SSTVSGAFNQ EVVEAMMQSC DRPMIFPLSN PTSRMEAMPA
DVLAWSGGKA LVTTGTPVAP VEYHDIAYTI GQANNVLVFP GIGLGVIVAG ARLLTQGMLR
AAAKALAHQA SPTTTGDSLL PDVQDLRGIS RTVAAAVYQA AVADNVATRI HADVGQAIRE
TMWLPEYD
//
