ID   D9Q0T1_ACIS3            Unreviewed;       451 AA.
AC   D9Q0T1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:ADL18919.1};
GN   OrderedLocusNames=ASAC_0512 {ECO:0000313|EMBL:ADL18919.1};
OS   Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 /
OS   345-15).
OC   Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC   Acidilobus.
OX   NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL18919.1, ECO:0000313|Proteomes:UP000000346};
RN   [1] {ECO:0000313|EMBL:ADL18919.1, ECO:0000313|Proteomes:UP000000346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16705 / JCM 18335 / VKM B-2471 / 345-15
RC   {ECO:0000313|Proteomes:UP000000346};
RX   PubMed=20581186; DOI=10.1128/AEM.00599-10;
RA   Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I.,
RA   Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "The genome sequence of the crenarchaeon Acidilobus saccharovorans supports
RT   a new order, Acidilobales, and suggests an important ecological role in
RT   terrestrial acidic hot springs.";
RL   Appl. Environ. Microbiol. 76:5652-5657(2010).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; CP001742; ADL18919.1; -; Genomic_DNA.
DR   RefSeq; WP_013266431.1; NC_014374.1.
DR   AlphaFoldDB; D9Q0T1; -.
DR   STRING; 666510.ASAC_0512; -.
DR   GeneID; 9498743; -.
DR   KEGG; asc:ASAC_0512; -.
DR   eggNOG; arCOG00853; Archaea.
DR   HOGENOM; CLU_034446_2_1_2; -.
DR   InParanoid; D9Q0T1; -.
DR   OrthoDB; 45556at2157; -.
DR   Proteomes; UP000000346; Chromosome.
DR   GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
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; 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   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   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000346}.
FT   DOMAIN          23..156
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          168..404
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
SQ   SEQUENCE   451 AA;  49377 MW;  C2ACE7CA509217DB CRC64;
     MAEEEEGTEE WYKLSTELHR FYGGKIEVLP KVPVRRLKDF AIWYTPGVAQ PSRLISSDPD
     LSFELTSRWN TIAVVSDGTR VLGLGKVGPE AAYPVMEGKA LLFKYLGGVD AVPIVHRARD
     AAKFVELLQL IEPSFGGINL EDIEKPKCFT ILDEARSKLQ IPVWHDDQQG TATAVLAGLI
     NALKVVGKKL QDVRIVLFGA GASNVAFYRL LKALGHNMHN VVAVTTKGVL HPEMKDIDKL
     MLTDPYQYQI AIETGGGGLP PNSPIEKAFD GADVVIAASV PGPGVIRPEW VSRMNRDAVV
     FALANPVPEI WPSEARRAGA RVVATGRSDF PNQVNNSLVF PAVFRGVLDV RARTITDTMA
     IAAAVELAKF AEERGGVGEE RILPTMEEWE VYPRVAAAVA VKAVEEGVAR RTTTYREELE
     RATEIIGTVR QKIQLLWGNG IIPKPPVDYQ G
//