ID O28547_ARCFU Unreviewed; 456 AA.
AC O28547;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=Malate oxidoreductase (Mae) {ECO:0000313|EMBL:AAB89524.1};
GN OrderedLocusNames=AF_1727 {ECO:0000313|EMBL:AAB89524.1};
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325 {ECO:0000313|EMBL:AAB89524.1, ECO:0000313|Proteomes:UP000002199};
RN [1] {ECO:0000313|EMBL:AAB89524.1, ECO:0000313|Proteomes:UP000002199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16
RC {ECO:0000313|Proteomes:UP000002199};
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.P., Clayton R.A., Tomb J., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B., Peterson S.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L., Utterback T., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; AE000782; AAB89524.1; -; Genomic_DNA.
DR PIR; F69465; F69465.
DR AlphaFoldDB; O28547; -.
DR STRING; 224325.AF_1727; -.
DR PaxDb; 224325-AF_1727; -.
DR EnsemblBacteria; AAB89524; AAB89524; AF_1727.
DR KEGG; afu:AF_1727; -.
DR eggNOG; arCOG00853; Archaea.
DR HOGENOM; CLU_034446_2_1_2; -.
DR PhylomeDB; O28547; -.
DR Proteomes; UP000002199; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000002199}.
FT DOMAIN 38..171
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 183..413
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
SQ SEQUENCE 456 AA; 50566 MW; 28C474AB10014D85 CRC64;
MYRVKTFKYY STYKICMIEE VFELTQNGRA KKWHAFYGGK IEILPKVPIR TLDDFSIWYT
PGVAEVCNEI AEDEEKAYDY TNKWNLIAII TDGSRTLGLG NIGPKAAMPV MEGKALLFKF
LGAVDAFPIA LAEQDADRFI EIVKAISPTF GGVNLEDISS PKCFYILERL QKELDIPVWH
DDQQGTATAT LAALINALKI VGKDISEVKI SIIGVGAANF ATIRLLKAAG ADPKKMFVVD
SKGILHPDRA DLKEKKGYKW QVAIETNGER RTGGMEEAIR GTDVLIAASK PGPDVIKKEW
IAEMNDDAIV FPLANPTPEI WPWEAKDAGA RIVGTGRSDF PNQVNNSLVF PGVFRGALTV
RARKITDEMC LAAANALAEF AERNGLSEDY IIPRMTEKEV FPEVATAVGV KAVELGLARL
ELREEEIYEI AELMISATQR KIKKLYELGF IKEPPS
//
