ID   G7VDT2_9CREN            Unreviewed;       434 AA.
AC   G7VDT2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:AET31514.1};
GN   ORFNames=P186_0045 {ECO:0000313|EMBL:AET31514.1};
OS   Pyrobaculum ferrireducens.
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=1104324 {ECO:0000313|EMBL:AET31514.1, ECO:0000313|Proteomes:UP000005867};
RN   [1] {ECO:0000313|EMBL:AET31514.1, ECO:0000313|Proteomes:UP000005867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1860 {ECO:0000313|EMBL:AET31514.1,
RC   ECO:0000313|Proteomes:UP000005867};
RX   PubMed=22247528; DOI=10.1128/JB.06465-11;
RA   Mardanov A.V., Gumerov V.M., Slobodkina G.B., Beletsky A.V.,
RA   Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "Complete genome sequence of strain 1860, a crenarchaeon of the genus
RT   pyrobaculum able to grow with various electron acceptors.";
RL   J. Bacteriol. 194:727-728(2012).
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}.
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DR   EMBL; CP003098; AET31514.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7VDT2; -.
DR   STRING; 1104324.P186_0045; -.
DR   KEGG; pyr:P186_0045; -.
DR   eggNOG; arCOG00853; Archaea.
DR   HOGENOM; CLU_034446_2_1_2; -.
DR   OrthoDB; 45556at2157; -.
DR   BioCyc; PSP1104324:GJSN-44-MONOMER; -.
DR   Proteomes; UP000005867; 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; 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;
FT   DOMAIN          17..150
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          162..395
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
SQ   SEQUENCE   434 AA;  47772 MW;  20F9AF134D6E36EB CRC64;
     MTEKWYQLSV EVHKKYGGKI SIIPKVPISS MEEFAIYYTP GIAEVSRQIH KNPELAFELT
     SRWNIIGVIT DGTRVLGLGN IGPEAAYPVM EGKALIFKYL GGVDAIPIPI RVKTPEEFIS
     VAKALEPALG GVNLEDIESP KCFYLLDKLR KELQIPVWHD DQQGTATATL AGLINALKLV
     GKKISDVTIA LVGAGASNIY TARILIKYGA KPGNLILVDS KGILHPERDD IDKMMIENPW
     KYKYAIETNA ERRRGGIPEA MKGADVIIAA SRPGPGVIKK EWVASMNKDA IVFALANPVP
     EIWPWEAKEA GAKIVATGRS DFPNQVNNSL IFPAVFRGAL DVRATTITDE MLIAAAEEVA
     KFAEEKGIHE EYIIPKMTEW EVYVREAAAV AATASAQKVA RIPRSYNEEL EVARTVIGKS
     IKTLEILMRE KIIE
//