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Database: UniProt
Entry: A0A133VFW2_9EURY
LinkDB: A0A133VFW2_9EURY
Original site: A0A133VFW2_9EURY 
ID   A0A133VFW2_9EURY        Unreviewed;       442 AA.
AC   A0A133VFW2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KXB05323.1};
GN   ORFNames=AKJ50_01235 {ECO:0000313|EMBL:KXB05323.1};
OS   candidate division MSBL1 archaeon SCGC-AAA382A13.
OC   Archaea; Euryarchaeota; candidate division MSBL1.
OX   NCBI_TaxID=1698279 {ECO:0000313|EMBL:KXB05323.1, ECO:0000313|Proteomes:UP000070311};
RN   [1] {ECO:0000313|EMBL:KXB05323.1, ECO:0000313|Proteomes:UP000070311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC-AAA382A13 {ECO:0000313|EMBL:KXB05323.1};
RX   PubMed=26758088; DOI=10.1038/srep19181;
RA   Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA   Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT   "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT   pools of the Red Sea.";
RL   Sci. Rep. 6:19181-19181(2016).
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}.
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:KXB05323.1}.
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DR   EMBL; LHYD01000019; KXB05323.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A133VFW2; -.
DR   PATRIC; fig|1698279.3.peg.105; -.
DR   Proteomes; UP000070311; Unassembled WGS sequence.
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; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000070311}.
FT   DOMAIN          21..157
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          169..398
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
SQ   SEQUENCE   442 AA;  48185 MW;  4C4B3A59943500FA CRC64;
     MLSEKEPNAT EVSNKYHKYY KGKFAIQSKV PVREEKADYD FSIWYTPGVA EPCKQIDKDK
     QNVYEYTNKG NMVAVVSDGT RILGLGSLGP EAAMPVMEGK SLLFKYLGNI DAVPVCIDTK
     DEDEIVDFVE KLQPTFGGIN LEDIEKPKCF KVLEKLRESL DIPVWHDDQQ GTALVSLAGL
     FGGLKFVGKK PEEIKLVIGG AGAAGINNAK YAITGGVKPE NVKIVDSKGI ISTSRDDIEE
     GTYKHEWAKR TNPENIEGDM KDALNGADAC ISATVPGPGI ITKEMVSGMA DDSILFAEAN
     PVPEILPEDA KEAGVRIVGT GRSDYPNQVN NSLGFPAVFR GALEVHATGI TDEMCGTAAY
     AIAERAEEIG LREDFVIPSM NDKEMYVKEA LAVAKKAMEQ GIARKKVGEK ELEERIRTKL
     DSAKNATQLL MQEGIIPDFP SD
//
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