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}.
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; 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
//