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Database: UniProt
Entry: A0A1X1RHM2_MYCCE
LinkDB: A0A1X1RHM2_MYCCE
Original site: A0A1X1RHM2_MYCCE 
ID   A0A1X1RHM2_MYCCE        Unreviewed;       397 AA.
AC   A0A1X1RHM2;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:ORV06343.1};
GN   ORFNames=AWB95_21845 {ECO:0000313|EMBL:ORV06343.1};
OS   Mycobacterium celatum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=28045 {ECO:0000313|EMBL:ORV06343.1, ECO:0000313|Proteomes:UP000193907};
RN   [1] {ECO:0000313|EMBL:ORV06343.1, ECO:0000313|Proteomes:UP000193907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44243 {ECO:0000313|EMBL:ORV06343.1,
RC   ECO:0000313|Proteomes:UP000193907};
RA   Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA   Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA   Olivier J., Enrico T., Nicola S.;
RT   "The new phylogeny of the genus Mycobacterium.";
RL   Submitted (JAN-2016) 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:ORV06343.1}.
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DR   EMBL; LQOM01000051; ORV06343.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1RHM2; -.
DR   STRING; 28045.AWB95_21845; -.
DR   Proteomes; UP000193907; 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   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}.
FT   DOMAIN          29..162
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          174..394
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        50
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        105
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         147
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         148
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         173
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   397 AA;  41156 MW;  3F5CDC9040723B01 CRC64;
     MSRSTLKDVS EPSPHIVLED EEIFEAHLAG KLSMQLRAPL DTQRALSIAY TPGVAQVSRA
     IAADHTLAAR YTWAHRLVAV VSDGSAVLGL GDIGAAAALP VMEGKCALFK AFAGLDSIPI
     VLDTKDPDEI IDTLVRLRPT FGAVNLEDIS APRCFEIERR LIEALDCPVM HDDQHGTAIV
     VLAALIGATK VLGRDMASLR VVISGVGAAG LACAKILMSV GISHITLLDS RGILHAGRDD
     LTTIKADLAR CSNPDGLTGG MVEALKGADM FLGVSGGVVP EELIATMAPD GIVFALSNPD
     PEIHPDVAAR HAAIVATGRS DFPNQINNVL AFPGVFLGAL DAGARRITEA MKVAAAEAIV
     SVVADDLAPD RIVPSPLDPR VGPAVAAAVA AAADTAE
//
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