ID A0A0F4JP95_9ACTN Unreviewed; 478 AA.
AC A0A0F4JP95;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KJY35573.1};
GN ORFNames=VR44_09845 {ECO:0000313|EMBL:KJY35573.1};
OS Streptomyces katrae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY35573.1, ECO:0000313|Proteomes:UP000033551};
RN [1] {ECO:0000313|EMBL:KJY35573.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY35573.1};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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:KJY35573.1}.
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DR EMBL; JZWV01000213; KJY35573.1; -; Genomic_DNA.
DR RefSeq; WP_042817021.1; NZ_JZWV01000213.1.
DR AlphaFoldDB; A0A0F4JP95; -.
DR STRING; 68223.GCA_002028425_02774; -.
DR PATRIC; fig|68223.7.peg.5515; -.
DR eggNOG; COG0281; Bacteria.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000033551; 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}.
FT DOMAIN 12..86
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 114
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 211
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 212
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 237
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 478 AA; 49227 MW; 490EC865DB07A5F1 CRC64;
MATAPSVSYS MTVRLEVPAS GTAVSQLTTA VESSGGSVTG LDVTASGHEK LRIDVTIAAT
STAHADEIVE KLRGIEGVSL GKVSDRTFLM HLGGKIEMSS KHPIRNRDDL SMIYTPGVAR
VCTAIAENPE DARRLTIKRN SVAVVTDGSA VLGLGNIGPM AALPVMEGKA ALFKRFAGID
AWPICLDTQD SDEIVAIVKA IAPGFAGINL EDISAPRCFE IEARLREALD IPVFHDDQHG
TAIVVLAALT NALRVVGKAV EDVKVVMSGA GAAGTAILKL LLAAGVKNAV SADIHGVVHA
GRPDLVDAAP DSPLRWIADN TNPEGYTGTL KEAVVGADVF IGVSAPNVLS GEDVAAMAEG
AIVFALANPD PEVDPAVARQ TAAVVATGRS DFPNQINNVL VFPGVFRGLL DAQSRTVNTD
MMLAAATALA DVVGRDELNA NYIIPSVFND KVAGAVAGAV RKAAQAGAEK AAVTGPTA
//
