ID A0A1E3THM0_MYCSH Unreviewed; 388 AA.
AC A0A1E3THM0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Malate dehydrogenase [Rhodococcus jostii RHA1] {ECO:0000313|EMBL:SRX94206.1};
GN ORFNames=MSP7336_02454 {ECO:0000313|EMBL:SRX94206.1};
OS Mycobacterium shimoidei.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=29313 {ECO:0000313|EMBL:SRX94206.1, ECO:0000313|Proteomes:UP000252015};
RN [1] {ECO:0000313|EMBL:SRX94206.1, ECO:0000313|Proteomes:UP000252015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P7336 {ECO:0000313|EMBL:SRX94206.1,
RC ECO:0000313|Proteomes:UP000252015};
RG IHU Genomes;
RL Submitted (MAY-2018) 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}.
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DR EMBL; UEGW01000001; SRX94206.1; -; Genomic_DNA.
DR RefSeq; WP_069395479.1; NZ_UEGW01000001.1.
DR AlphaFoldDB; A0A1E3THM0; -.
DR STRING; 29313.BHQ16_07860; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000252015; 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 21..154
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 166..386
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 42
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 140
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 165
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 388 AA; 40225 MW; EADE29A9B85DEADB CRC64;
MSETNAHIEL EDEEIFEAHV AGKLRVESRT PLDTQRALSI AYTPGVAQVS RAIAADHTLA
ARYTWANRLV AVVSDGSAVL GLGDIGAAAA LPVMEGKCAL FKAFAGLDAI PIVLDTKDPD
EIVDTLVRLR PTFGAVNLED ISAPRCFEIE RRLIDALDCP VMHDDQHGTA IVVLAALIGA
TKVLGRDMTA LRVVISGVGA AGLACAKILM SVGISHITLL DSRGILHPGR DDLTTVKADL
AQCTNPDGLT GGMVEALKGA DVFLGVSAGI VPEELIATMA PHSIVFALSN PDPEIHPEQA
ARHAAIVATG RSDFPNQINN VLAFPGVFLG ALDAGARKIT EAMKVAAAEA IVSVVADDLA
PDRIVPSPLD PRVGPAVAAA VAATAAAE
//
