ID L9WFG0_9EURY Unreviewed; 751 AA.
AC L9WFG0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Bifunctional malic enzyme oxidoreductase/phosphotransacetylase {ECO:0000313|EMBL:ELY48250.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:ELY48250.1};
GN ORFNames=C495_02210 {ECO:0000313|EMBL:ELY48250.1};
OS Natronorubrum sulfidifaciens JCM 14089.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronorubrum.
OX NCBI_TaxID=1230460 {ECO:0000313|EMBL:ELY48250.1, ECO:0000313|Proteomes:UP000011661};
RN [1] {ECO:0000313|EMBL:ELY48250.1, ECO:0000313|Proteomes:UP000011661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14089 {ECO:0000313|EMBL:ELY48250.1,
RC ECO:0000313|Proteomes:UP000011661};
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:ELY48250.1}.
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DR EMBL; AOHX01000025; ELY48250.1; -; Genomic_DNA.
DR RefSeq; WP_008159603.1; NZ_AOHX01000025.1.
DR AlphaFoldDB; L9WFG0; -.
DR STRING; 1230460.C495_02210; -.
DR PATRIC; fig|1230460.4.peg.443; -.
DR eggNOG; arCOG00853; Archaea.
DR OrthoDB; 45556at2157; -.
DR Proteomes; UP000011661; 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:ELY48250.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011661}.
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"
SQ SEQUENCE 751 AA; 81261 MW; 87D84A3F6AD35F18 CRC64;
MGLDEDSLEY HRTDPPGKIE ISTTKPTNTQ RDLSLAYSPG VAAPCLEIDE DEADAYTYTA
KGNLVGVVSN GSAVLGLGDI GAQASKPVME GKGVLFKRFA DIDVFDIELD EADPDKLVEA
VKMMEPTFGG INLEDIKAPE CFTVEERLRE ELDIPVFHDD QHGTAIISGA ALLNAADVAG
KDLEDLEITF SGAGASAIAT ARFYVSLGVR KENITMCDST GIITDERAES GDINEYKQQF
ARDVSDGSLA DAMEDADVFV GLSAGGIVSQ EMVASMADNP IIFAMANPDP EIGYEEAKAA
RDDDVIMATG RSDYPNQVNN VLGFPFIFRG ALDVRATEIN EEMKVACAEA LADLARQDVP
DAVVKAYGDD PLQFGPDYII PKPVDPRVLF RVAPSIAEAA MDSGAARTEI DLEAYEEELE
ARLGKSREMM RVVLNKAKSD PKTVALAEGE NEKMIRAAYQ IQEQGIALPI LIGDEHEIRQ
TATDLGLDFD PQVADPSVGD YEGYADRLHE LRARKGVTRT EAGELIERDS NYFGSVMVEQ
GDADALLTGL SHHYPSALRP PLQVIGTDDD VDYAAGVYML TFKNRVIFVA DATVNQDPDE
DVLAEVTRQT GKLARRFNVE PRAALLSYSN FGSVNNEGTR KPRRAAAMLQ DDPEIDFPVD
GEMQADTAVV EDILEGTYGF SELDEPANVL VFPNLESGNI GYKLLQRLGG ADAIGPMLVG
MDEPVHVLQR GDEVKDIVNL AGVAVVDAQK E
//
