ID M0D2M3_9EURY Unreviewed; 750 AA.
AC M0D2M3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Bifunctional malic enzyme oxidoreductase/phosphotransacetylase {ECO:0000313|EMBL:ELZ29073.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:ELZ29073.1};
GN ORFNames=C473_14699 {ECO:0000313|EMBL:ELZ29073.1};
OS Halorubrum terrestre JCM 10247.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum; Halorubrum distributum group.
OX NCBI_TaxID=1227486 {ECO:0000313|EMBL:ELZ29073.1, ECO:0000313|Proteomes:UP000011572};
RN [1] {ECO:0000313|EMBL:ELZ29073.1, ECO:0000313|Proteomes:UP000011572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10247 {ECO:0000313|EMBL:ELZ29073.1,
RC ECO:0000313|Proteomes:UP000011572};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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 -!- 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:ELZ29073.1}.
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DR EMBL; AOIW01000074; ELZ29073.1; -; Genomic_DNA.
DR RefSeq; WP_007346072.1; NZ_AOIW01000074.1.
DR AlphaFoldDB; M0D2M3; -.
DR PATRIC; fig|1227486.3.peg.2855; -.
DR Proteomes; UP000011572; Unassembled WGS sequence.
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:ELZ29073.1}.
FT DOMAIN 16..149
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 161..401
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 750 AA; 81174 MW; FDA4DF4466D60FB3 CRC64;
MGLDDDAREY HRQEPPGKIA IETTKPTNTQ RDLSLAYSPG VAAPCRDIAA DPESVFEYTA
KGNLVAVVSN GSAVLGLGDI GAAASKPVME GKGVLFKRFA DIDVFDIELD IDSVDPFCEA
VKAMEPTFGG INLEDIKAPE CFKIEERLRE EMDVPVFHDD QHGTAIISGA ALMNAVDISD
KDLSELEIVF SGAGASAIAT ARFYVSLGAR KENITMCDSS GIITEERVEA GEVNEYKSQF
ATPVEGGDLA DAMEGADVFV GLSVGGIVSQ EMVRSMGDDP IIFAMANPDP EITYEDAKDA
RDDTVIMATG RSDYPNMVNN VLGFPFLFRG ALDVRATEIN EEMKAAAAEA LADLARKDVP
DAVVKAYGDE PLQFGPDYVI PKPLDPRVLF EVAPRVAEAA MESGSARAEI DLEKYRERLE
ARLGKSREMM RVVLNKAKSD PKRIALAEGT DEKMIRAAYQ LSEQGIAEPV LLGDADTISQ
TAAELGLSFR PEVVDPDDRD VSGYGDRLYE LRKRKGITKR EADDLVKRDT NYLGSVMVET
GDVDAMLTGL THHYPSALRP PLQIVGSAAD TDTVAGVYML TFKNRVIFCA DTTVNQDPDA
ETLAEVTRHT ADLARRFNVE PRAAMLSYSN FGSVDNEGTR KPRDAVDILQ SDDAVDFPVD
GEMQADTAVV DDILNGTYEF SQLDEAANVL VFPNLEAGNI GYKLLQRLGG AEAIGPMLVG
MDEPVHVLQR GDEVKDIVNL ASVAVVDAQE
//
