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Database: UniProt
Entry: A0A249KQR8_9ACTN
LinkDB: A0A249KQR8_9ACTN
Original site: A0A249KQR8_9ACTN 
ID   A0A249KQR8_9ACTN        Unreviewed;       458 AA.
AC   A0A249KQR8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) {ECO:0000313|EMBL:ASY19124.1};
GN   ORFNames=A1sIA105_06375 {ECO:0000313|EMBL:ASY19124.1};
OS   Candidatus Planktophila versatilis.
OC   Bacteria; Actinomycetota; Actinomycetes; Candidatus Nanopelagicales;
OC   Candidatus Nanopelagicaceae; Planktophila.
OX   NCBI_TaxID=1884905 {ECO:0000313|EMBL:ASY19124.1, ECO:0000313|Proteomes:UP000217175};
RN   [1] {ECO:0000313|EMBL:ASY19124.1, ECO:0000313|Proteomes:UP000217175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS-IA-105 {ECO:0000313|EMBL:ASY19124.1};
RA   Neuenschwander S.M., Salcher M., Ghai R., Pernthaler J.;
RT   "High microdiversification within the ubiquitous acI lineage of
RT   Actinobacteria.";
RL   Submitted (JUL-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}.
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DR   EMBL; CP016775; ASY19124.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A249KQR8; -.
DR   Proteomes; UP000217175; 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   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; 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.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW   ECO:0000256|RuleBase:RU003427}.
FT   DOMAIN          92..225
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          237..458
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        113
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         210
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         211
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         236
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         362
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         391
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   458 AA;  48304 MW;  230E44B253E4DE3F CRC64;
     MASTSPGYGI TIRVEGSPEL QPVALITTTI TNAGATITAL DVVESLLEKV VIDVTCDTID
     SDHAQQIHDA LSANNGLTVR KVSDRTFLLH LGGKIEVTSK VPLKTRDDLS RAYTPGVARI
     SQAIVDDPSD VRRLTMKRNT VAVVTDGSAV LGLGNIGPAA ALPVMEGKAA LFKRFANVDA
     WPVCLDTQDV DEIVRTVQLI APVYGGINLE DISAPRCFEV ERRLRELLDI PVFHDDQHGT
     AIVVLAALRN ALKLVKKEMS AVKIVMSGAG AAGTAIARLL LLSGAQNITA FDKDGLIGGD
     SKSSDPMRSW FIEHSNPGNF AGDIHQAMVG ADIFIGVSAP HVLKEADVAA MAAGSIVFAL
     ANPDPEIDPV IARKYATVVA TGRSDHPNQI NNVLAFPGIF RGLLDAQAHK ITDKLLVAAA
     EAIADCVSPS QLNTSFIVPS VFDPNVVVKV AAAVKASV
//
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