ID M0P0Y5_9EURY Unreviewed; 750 AA.
AC M0P0Y5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Bifunctional malic enzyme oxidoreductase/phosphotransacetylase {ECO:0000313|EMBL:EMA63822.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:EMA63822.1};
GN ORFNames=C468_09469 {ECO:0000313|EMBL:EMA63822.1};
OS Halorubrum kocurii JCM 14978.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1230456 {ECO:0000313|EMBL:EMA63822.1, ECO:0000313|Proteomes:UP000011546};
RN [1] {ECO:0000313|EMBL:EMA63822.1, ECO:0000313|Proteomes:UP000011546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14978 {ECO:0000313|EMBL:EMA63822.1,
RC ECO:0000313|Proteomes:UP000011546};
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:EMA63822.1}.
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DR EMBL; AOJH01000060; EMA63822.1; -; Genomic_DNA.
DR RefSeq; WP_008848609.1; NZ_AOJH01000060.1.
DR AlphaFoldDB; M0P0Y5; -.
DR STRING; 1230456.C468_09469; -.
DR PATRIC; fig|1230456.3.peg.1868; -.
DR OrthoDB; 45556at2157; -.
DR Proteomes; UP000011546; 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:EMA63822.1}.
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"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 750 AA; 81232 MW; 7F52201423780CDA CRC64;
MGLDDDAREY HRREPPGKIE IETTKPTNTQ RDLSLAYSPG VAAPCRDIAA DPDSVFEYTA
KGNLVAVVSN GSAVLGLGDI GASASKPVME GKGVLFKRFA DIDVFDIELE IDDVDPFCEA
VKAMEPTFGG VNLEDIKAPE CFKIEERLRE EMDVPVFHDD QHGTAIISGA ALMNATEISG
KDLSEIEIVF SGAGASAIAT ARFYVSLGAK RENITMCDSS GVITEDRVAN GDVNEYKSQF
ASEGEGGDLA DAMAGADVFV GLSVGGIVSQ EMVRSMASDP IIFAMANPDP EITYEDAKDA
RDDTVIMATG RSDYPNMVNN VLGFPFLFRG ALDVRATEIN EEMKRAAAEA LAELARKDVP
DAVVKAYGDD PLQFGPDYVI PKPLDPRVLF EVAPSVAKAA MESGCARTEI DLETYREQLE
ARLGKSREMM RVVLNKAKSD PKRIALAEGT DEKMIRAAYQ LSEQGIADPV LLGDADEIAR
TADALGLSFR PEIVDPADRD VSAYGNQLYQ LRKRKGITSR EANELVRRDT NYLGSVMVKS
GDVDAMLTGL THHYPSALRP PLQVIGSAAD TDTVAGVYML TFKNRVVFCA DTTVNQDPDA
ETLAEITRHT ADLARRFNVE PRAAMLSYSN FGSVDNEGTQ KPRDAVEILH EDEEVDFPVD
GEMQADTAVV DEILNDTYEF SQLDEAANVL VFPNLEAGNI GYKLLQRLGG AEAIGPMLVG
MDQPVHVLQR GDEVKDIVNL ASVAVVDAQE
//
