ID A0A170U665_9ACTN Unreviewed; 461 AA.
AC A0A170U665;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:GAT79362.1};
GN ORFNames=STXM2123_63 {ECO:0000313|EMBL:GAT79362.1};
OS Streptomyces sp. F-3.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1840095 {ECO:0000313|EMBL:GAT79362.1, ECO:0000313|Proteomes:UP000078145};
RN [1] {ECO:0000313|EMBL:GAT79362.1, ECO:0000313|Proteomes:UP000078145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wang L.S., Gao P.J., Liu L., Zhang H.Q., Cheng Z., Sun X.M.;
RT "Streptomyces sp. F-3 geneom sequencing.";
RL Submitted (MAY-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 -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003427}.
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:GAT79362.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BDDR01000001; GAT79362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A170U665; -.
DR STRING; 1840095.STXM2123_63; -.
DR Proteomes; UP000078145; 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; IPR002912; ACT_dom.
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; 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; PS51671; ACT; 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:UP000078145}.
FT DOMAIN 2..76
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 104
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 201
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 202
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 227
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 387
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 461 AA; 48201 MW; 0E6ADA9EAD7A2A56 CRC64;
MTIRLEVPAG GTAVSQLTTA VESSGGSVTG LDVTASGHER LRIDVTIAAT STTHAQEIIE
KLRGIEGVTL GKVSDRTFLM HLGGKIEMAS KHPIRNRDDL SMIYTPGVAR VCMAIAENPE
DARRLTIKRN SVAVVTDGSA VLGLGNIGPK AALPVMEGKA ALFKRFAGID AWPLCLDTQD
VDEIVRIVKA IAPGFAGINL EDISAPRCFE IEARLREALD IPVFHDDQHG TAIVVLAALT
NALRVVGKEI DSVRVVMSGA GAAGTAILKL LLAAGVKNAV VADIHGVVHA DREDLVDAAP
DSALRWIAEN TNPENLTGTL KEAVRGADVF IGVSAPNVID GDDVAAMADG AIVFALANPD
PEVDPAIARE TAAVVATGRS DFPNQINNVL VFPGVFRGLL DAQSRSVNME MMLAAAQALA
DVVTEDELNP NYIIPSVFND RVASTVAGAV RAAAERSGAT A
//
