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Database: UniProt
Entry: A0A2U1FRQ8_9PSEU
LinkDB: A0A2U1FRQ8_9PSEU
Original site: A0A2U1FRQ8_9PSEU 
ID   A0A2U1FRQ8_9PSEU        Unreviewed;       421 AA.
AC   A0A2U1FRQ8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) {ECO:0000313|EMBL:PVZ14857.1};
GN   ORFNames=C8D89_101725 {ECO:0000313|EMBL:PVZ14857.1};
OS   Actinomycetospora cinnamomea.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinomycetospora.
OX   NCBI_TaxID=663609 {ECO:0000313|EMBL:PVZ14857.1, ECO:0000313|Proteomes:UP000245639};
RN   [1] {ECO:0000313|EMBL:PVZ14857.1, ECO:0000313|Proteomes:UP000245639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45771 {ECO:0000313|EMBL:PVZ14857.1,
RC   ECO:0000313|Proteomes:UP000245639};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:PVZ14857.1}.
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DR   EMBL; QEKW01000001; PVZ14857.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1FRQ8; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000245639; 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; 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   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|RuleBase:RU003427};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245639}.
FT   DOMAIN          37..170
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          182..404
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   421 AA;  43770 MW;  889169C73359B7C8 CRC64;
     MSDPAGPTVD STDTTDNQPH LDGRDITEEE VFAAHEAGKL SVAPTVGLAG RRDLAIAYTP
     GVAKVCRAIA DDKALTARYT WTHRLVAVVS DGTAVLGLGD IGPRASLPVM EGKSALFKAF
     ADLDSIPLVL ETTDVDEIVD TLVHLRPSFG AVNLEDIAAP RCFEIERRLI EALDCPVMHD
     DQHGTAIVVL AALRNAVRVL DRDLASLRVV VSGAGASGVA CAKILMLAGA SDVVVLDSRG
     VIHAGREGMN VEKIALAEQT NPRGVRGDLA TALEGADVFL GLSGSTVPEA VIASMADDAI
     VFALSNPDPE IDPAVARKHA AVVATGRSDY PNQINNVLAF PGVFAGALDA AARRITEAMK
     LAAAEAIADI AAGDEEFGRD HIVPSALDPC VAPAVAEAVA RAAAEEGVVR RHVAEVAAEH
     R
//
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