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Database: UniProt
Entry: B1L5G7_KORCO
LinkDB: B1L5G7_KORCO
Original site: B1L5G7_KORCO 
ID   B1L5G7_KORCO            Unreviewed;       460 AA.
AC   B1L5G7;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) {ECO:0000313|EMBL:ACB07696.1};
DE            EC=1.1.1.38 {ECO:0000313|EMBL:ACB07696.1};
GN   OrderedLocusNames=Kcr_0950 {ECO:0000313|EMBL:ACB07696.1};
OS   Korarchaeum cryptofilum (strain OPF8).
OC   Archaea; Candidatus Korarchaeota; Candidatus Korarchaeum.
OX   NCBI_TaxID=374847 {ECO:0000313|EMBL:ACB07696.1, ECO:0000313|Proteomes:UP000001686};
RN   [1] {ECO:0000313|EMBL:ACB07696.1, ECO:0000313|Proteomes:UP000001686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OPF8 {ECO:0000313|Proteomes:UP000001686};
RX   PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA   Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA   Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA   Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA   Richardson P., Keller M., Stetter K.O.;
RT   "A korarchaeal genome reveals new insights into the evolution of the
RT   Archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008).
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DR   EMBL; CP000968; ACB07696.1; -; Genomic_DNA.
DR   RefSeq; WP_012309593.1; NC_010482.1.
DR   AlphaFoldDB; B1L5G7; -.
DR   STRING; 374847.Kcr_0950; -.
DR   EnsemblBacteria; ACB07696; ACB07696; Kcr_0950.
DR   GeneID; 6094227; -.
DR   KEGG; kcr:Kcr_0950; -.
DR   eggNOG; arCOG00853; Archaea.
DR   HOGENOM; CLU_034446_2_1_2; -.
DR   InParanoid; B1L5G7; -.
DR   OMA; LVHDYTW; -.
DR   OrthoDB; 45556at2157; -.
DR   PhylomeDB; B1L5G7; -.
DR   Proteomes; UP000001686; Chromosome.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
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   Oxidoreductase {ECO:0000313|EMBL:ACB07696.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001686}.
FT   DOMAIN          30..163
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          175..407
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
SQ   SEQUENCE   460 AA;  51185 MW;  2384A5F542B8BD37 CRC64;
     MVERKPTVEE LLKKAERPSK LAVPYHQFYE GKVQVMPKCA IRTLDDFSIW YTPGVAAACK
     EIKADPDKSF FLTNRWNYVA VVSDGTRVLG LGNIGPEAGL PVMEGKALLF KYLGGVDAFP
     LVVRAHDPDD MIKLLEWVEP NFGGVNLEDI EKPKCYYVLE EARKRLQIPV WHDDQQGTAT
     VTYAGLVNAF KLVGKKMKDS KIVLYGAGAA NVRTAIVLIT AGVPPGNIVM IDTVGPLYRD
     RPDIEEMKKE DRWKYDLAMK TNKENNKTIE EAFKGADAVV GASKPGPGVI KQEWIKLMNK
     DPIVFACANP IPEIWPWEAK EAGAKIVATG RSDFPNQVNN SLAFPAIFRG VLDVRAKTVT
     DEMCIAAGDA LAKFAEEKGL REDYILPTMD DWEVYPIEAV AAAEQSIKQG VARRILSREE
     LYERAVNIIR NARESARFLM EKGLISSPPP EEDVLRSYGP
//
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