ID   G0LLR9_HALWC            Unreviewed;       748 AA.
AC   G0LLR9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) {ECO:0000313|EMBL:CCC40875.1};
DE            EC=1.1.1.40 {ECO:0000313|EMBL:CCC40875.1};
GN   Name=maeB {ECO:0000313|EMBL:CCC40875.1};
GN   Synonyms=mdh2 {ECO:0000313|EMBL:CCC40875.1};
GN   OrderedLocusNames=Hqrw_3088 {ECO:0000313|EMBL:CCC40875.1};
OS   Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=768065 {ECO:0000313|EMBL:CCC40875.1, ECO:0000313|Proteomes:UP000007954};
RN   [1] {ECO:0000313|EMBL:CCC40875.1, ECO:0000313|Proteomes:UP000007954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16854 / JCM 12705 / C23
RC   {ECO:0000313|Proteomes:UP000007954};
RX   PubMed=21701686; DOI=10.1371/journal.pone.0020968;
RA   Dyall-Smith M., Pfeiffer F., Klee K., Palm P., Gross K., Schuster S.C.,
RA   Rampp M., Oesterhelt D.;
RT   "Haloquadratum walsbyi: limited diversity in a global pond.";
RL   PLoS ONE 6:E20968-E20968(2011).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC       family. {ECO:0000256|ARBA:ARBA00007686}.
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; FR746099; CCC40875.1; -; Genomic_DNA.
DR   RefSeq; WP_014556384.1; NC_017459.1.
DR   AlphaFoldDB; G0LLR9; -.
DR   GeneID; 12447867; -.
DR   KEGG; hwc:Hqrw_3088; -.
DR   HOGENOM; CLU_012366_0_0_2; -.
DR   OrthoDB; 45556at2157; -.
DR   Proteomes; UP000007954; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   CDD; cd05311; NAD_bind_2_malic_enz; 1.
DR   Gene3D; 3.40.50.10950; -; 1.
DR   Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 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; IPR012188; ME_PTA.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR042113; P_AcTrfase_dom1.
DR   InterPro; IPR042112; P_AcTrfase_dom2.
DR   InterPro; IPR002505; PTA_PTB.
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   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF036684; ME_PTA; 1.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000313|EMBL:CCC40875.1}.
FT   DOMAIN          16..149
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          161..398
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   748 AA;  80729 MW;  8BD4EAD8E9295318 CRC64;
     MGLEDDARDY HREDPSGKLE ISTTKPTNTQ RDLSLAYSPG VAAPCRDIAE DSTRGYEYTA
     KGNLVAVVSN GSAVLGLGDI GAQASKPVME GKGVLFKRFA DIDVFDLELD LADPTDIINS
     VSAMEPTFGG INLEDIKAPE CFEIESQLRE EMDIPVFHDD QHGTAIISGA ALLNAADIVG
     KDLSELNIVF SGAGASAIST ARFYLSLGAK KENIIMCDSS GVISSDRESL NRYKSEFAAD
     VPAETLAEAM EGADVFVGLS VGGIVSEEMI ASMAADPIVF AMANPDPEIG YVEAKNARDD
     TVVMATGRSD YPNQVNNVLG FPFIFRGALD VRATEINETM KRAAAEALAD LARQDVPDAV
     VKAYGEQPLQ FGPEYLIPKP VDPRVLFEVA PAVAQAAIES GCARRDIDTD IYEEQLEARL
     GKSREMMRVV LNKAKSNPKR VALAEGHDEK IIRAAYQMHE QGIAQPILVG DKSEIVATAS
     ELGLEFGPEI VDPSDETWDH YTDRLYELRR RKGVTRNEAE ELISGNSNYF ASVMVEQGDA
     DAMLTGLTHH YPSALRPPLQ VIGTAPEADY AAGVYLLTFK NQVVFAADTT VNLAPEADVL
     AEITKHTASL ARRFNIEPRA AMLSYSNFGS VENDGTKRLQ DAVTSLHDDP AVDFPVDGEM
     QADTAVIEDI LTETYDFSDL DEPANVLVFP NLEAGNIGYK LLQRLGGAEA IGPMLVGMDK
     PVHVLQRGDE VKDIVNLAGV AVVDAQND
//